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	<id>https://teaching.ncl.ac.uk/bms/wiki//api.php?action=feedcontributions&amp;feedformat=atom&amp;user=Nnjm2</id>
	<title>The School of Biomedical Sciences Wiki - User contributions [en]</title>
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	<updated>2026-04-12T03:13:59Z</updated>
	<subtitle>User contributions</subtitle>
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	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=James_Watson&amp;diff=23709</id>
		<title>James Watson</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=James_Watson&amp;diff=23709"/>
		<updated>2019-01-18T13:33:14Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;James Watson was a scientist at Cambridge University. He, along with [[Francis Crick|Francis Crick]], proposed the 3-D model and [[Double helix|double helix]] structure of [[Deoxyribonucleic acid|deoxyribonucleic acid]]&amp;amp;nbsp;(DNA). They put forward their theory in 1953&amp;lt;ref&amp;gt;Hartl. D.L. and Ruvolo M. (2012) Genetics: analysis of genes and genomes, 8th edition, United States of America: Jones and Bartlett Learning&amp;lt;/ref&amp;gt;. [[Watson-Crick base pairing|Watson-Crick base pairing]] is another name for [[Complementary base pairing|complementary base pairing]]&amp;lt;ref&amp;gt;Hartl. D.L. and Ruvolo M. (2012) Genetics: analysis of genes and genomes, 8th edition, United States of America: Jones and Bartlett Learning&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=James_Watson&amp;diff=23708</id>
		<title>James Watson</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=James_Watson&amp;diff=23708"/>
		<updated>2019-01-18T13:33:02Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;James Watson was a scientist at Cambridge University. He, along with [[Francis Crick|Francis Crick]], proposed the 3-D model and [[Double helix|double helix]] structure of [[Deoxyribonucleic acid|deoxyribonucleic acid]](DNA). They put forward their theory in 1953&amp;lt;ref&amp;gt;Hartl. D.L. and Ruvolo M. (2012) Genetics: analysis of genes and genomes, 8th edition, United States of America: Jones and Bartlett Learning&amp;lt;/ref&amp;gt;. [[Watson-Crick base pairing|Watson-Crick base pairing]] is another name for [[Complementary base pairing|complementary base pairing]]&amp;lt;ref&amp;gt;Hartl. D.L. and Ruvolo M. (2012) Genetics: analysis of genes and genomes, 8th edition, United States of America: Jones and Bartlett Learning&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Anion&amp;diff=23707</id>
		<title>Anion</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Anion&amp;diff=23707"/>
		<updated>2019-01-18T13:32:23Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;An anion is an [[Ion|ion]] with a net negative charge&amp;lt;ref&amp;gt;The Editors of Encyclopaedia Britannica. Anion. 1998 [Cited 5/12/18]; Available from: https://www.britannica.com/science/anion&amp;lt;/ref&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
=== References&amp;amp;nbsp;  ===&lt;br /&gt;
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&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Proton&amp;diff=23706</id>
		<title>Proton</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Proton&amp;diff=23706"/>
		<updated>2019-01-18T13:31:53Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;Positively charged [[Subatomic particles|subatomic particles]]&amp;amp;nbsp;which are found in the [[Nucleus|nucleus]] of [[Atom|atoms]]. A [[Hydrogen|hydrogen]] atom contains 1 proton and 1 [[Electron|electron]] therefore a 1+hydrogen ion/ H&amp;lt;sup&amp;gt;+&amp;lt;/sup&amp;gt;&amp;amp;nbsp;(which has lost its electron) can be said to be a proton.&amp;amp;nbsp; &lt;br /&gt;
&lt;br /&gt;
A proton is a subatomic particle with a [[Charges|charge]] of +1.60 x 10&amp;lt;sup&amp;gt;-19&amp;amp;nbsp;&amp;lt;/sup&amp;gt;c and a [[Mass|mass]] of 1.67 x 10&amp;lt;sup&amp;gt;-27&amp;amp;nbsp;&amp;lt;/sup&amp;gt;kg. It is a baryon and so consists of 3 [[Quarks|quarks]], two [[Up quarks|up quarks]] and one [[Down quarks|down quark]], it can therefore feel the [[Strong nuclear force|strong nuclear force]]. It&#039;s [[Antiparticle|antiparticle]] is the [[Antiproton|antiproton]].&amp;amp;nbsp;&amp;lt;sup&amp;gt;&amp;lt;/sup&amp;gt; &lt;br /&gt;
&lt;br /&gt;
The [[Isotope|isotope]] of [[Hydrogen|hydrogen]]- H&amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;&amp;lt;sub&amp;gt;1, &amp;lt;/sub&amp;gt;also known as [[Protium|protium]], is made up of one proton (no electrons) and so is the lightest [[Element|element]].&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=T_tubule&amp;diff=23705</id>
		<title>T tubule</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=T_tubule&amp;diff=23705"/>
		<updated>2019-01-18T13:31:27Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;T-tubules or transverse tubules run perpendicular to the long axis of the fibres in the [[Myofibrils|myofibrils]] of [[Skeletal Muscle|skeletal muscle]] and are invaginations in the [[Sarcolemma|sarcolemma]]. The tubules enter the sarcoplasm and extend over the sarcoplasmic reticulum at the junctions of the A and I bands. On either side of the T-tubules, the area that is associated with regions of the [[Sarcoplasmic Reticulum|sarcoplasmic reticulum]] is known as the terminal cisternae. The T-tubules and the terminal cisternae do not touch, however, but each T-tubule is associated with two terminal cisternae, and the three structures together are known as a triad&amp;lt;ref&amp;gt;http://www.getbodysmart.com/ap/muscletissue/fibers/sr/tutorial.html&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
When the T- tubule is depolarised due to an incoming [[Action potential|action potential]] in the sarcolemma, the impulse is carried down the t-tubules and opens the gates in the sarcoplasmic reticulum on the associated terminal [[Cisternae|cisternae]], releasing calcium ions. [[Calcium|Calcium]] ions flow into the [[Cytoplasm|cytoplasm]] where the actin and myosin filaments are. The calcium ions bind to the troponin-tropomyosin molecules located on the actin filaments and the power stroke is able to occur&amp;lt;ref&amp;gt;http://web.archive.org/web/20080401093325/http://www.lib.mcg.edu/edu/eshuphysio/program/section2/2ch3/communic.htm&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
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&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Posterior_pituitary_gland&amp;diff=23704</id>
		<title>Posterior pituitary gland</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Posterior_pituitary_gland&amp;diff=23704"/>
		<updated>2019-01-18T13:31:03Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: Cleaned up the text. Added some links.&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;The pituitary gland is part of the [[endocrine system|endocrine system]] and consists of two lobes: the posterior pituitary gland and the anterior pituiitary gland. &lt;br /&gt;
&lt;br /&gt;
The posterior pituitary gland, otherwise known as the neurohypophysis, is or neural origin. It is not a gland, despite the name, but in fact it is a large cluster of [[Axon|axons]] from the [[hypothalamus|hypothalamus]] that terminate behind the anterior pituitary gland. These axons then release [[hormones|hormones]] into the capillaries of the hypophyseal circulation&amp;lt;ref&amp;gt;Boundless anatomy and physiology. The Pituitary Gland. [Cited 05/12/18]; Available from: https://courses.lumenlearning.com/boundless-ap/chapter/the-pituitary-gland/&amp;lt;/ref&amp;gt;. such as [[oxytocin|oxytocin]]. &lt;br /&gt;
&lt;br /&gt;
=== References ===&lt;br /&gt;
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&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=P-type_pumps&amp;diff=23703</id>
		<title>P-type pumps</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=P-type_pumps&amp;diff=23703"/>
		<updated>2019-01-18T13:29:37Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;P-type pumps are a form of [[ATP-ase|ATPases]] which, during the [[Active transport|active transport]] of ions, are [[Phophorylation|phophorylated]] by themselves which is a process that is done reversibly&amp;lt;ref&amp;gt;Becker W.M., Kleinsmith L.J., Hardin J., Bertoni G.P. (2009) The World of the Cell, 7th Edition, San Francisco, Pearson Education. Pg 210&amp;lt;/ref&amp;gt;. They are classed in the [[Multipass membrane protein|multipass membrane protein]] group&amp;lt;ref&amp;gt;Alberts B., Johnson A., Lewis J., Raff M., Roberts K., Walter P. (2008) Molecular Biology of the Cell, 5th Edition, New York, Garland Science. Pg 659&amp;lt;/ref&amp;gt;. Examples of this type of pump are the [[Na+/K+ ATPase pump|Na&amp;lt;sup&amp;gt;+&amp;lt;/sup&amp;gt;/K&amp;lt;sup&amp;gt;+&amp;lt;/sup&amp;gt; pump]] and the [[Ca2+ pump|Ca&amp;lt;sup&amp;gt;2+&amp;lt;/sup&amp;gt; pump]]. &lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
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&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Bzip&amp;diff=23702</id>
		<title>Bzip</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Bzip&amp;diff=23702"/>
		<updated>2019-01-18T13:29:05Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;Bzip (Basic leucine zipper) is a [[Eukaryotic|eukaryotic]] [[Transcription factor|transcription factor]]. It consists of 2 regions. One basic region which interacts with [[DNA|DNA]], and the &#039;zipper&#039; region. This region contains a [[Leucine|leucine]] every 7 residues, forming an [[Alpha-helix|alpha-helix]] and is involved in dimerisation. These leucine zipper proteins, therefore, bind to [[DNA|DNA]] as dimers and grip to the [[Double helix|double helix]]&amp;lt;ref&amp;gt;Alberts B, Bray D, Hopkin K, Johnson A, Lewis J, Raff M, Roberts K, Walter P. Essential Cell Biology. 4th Edition. New York. Garland Science. 2013. p.267&amp;lt;/ref&amp;gt;. Members of the bZip family of [[Transcription factors|transcription factors bind]] to target sequences in the [[DNA|DNA]] such as homodimers and heterodimers that recognise [[Palindromic sequence|palindromic sequences]]. This affects developmental processes such as dendritic cell development, myeloid differentiation and brain development&amp;lt;ref&amp;gt;R&amp;amp;amp;amp;amp;D Systems. Basic Leucine Zipper (bZip) Transcription Factors. Available from: https://www.rndsystems.com/research-area/basic-leucine-zipper--bzip--transcription-factors  Cited: 20/11/17&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Glycolysis&amp;diff=23701</id>
		<title>Glycolysis</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Glycolysis&amp;diff=23701"/>
		<updated>2018-12-17T13:24:28Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;Glycolysis is the [[Metabolic process|metabolic process]] by which [[Glucose|glucose]] is converted to [[Pyruvate|pyruvate]] (also known as pyruvic acid). It is the first of the three stages of [carbohydrate metabolism]. The process of glycolysis is important in producing energy for the [[Cell|cell]], particularly in [[Anaerobic|anaerobic]] conditions. It occurs in the [[Cytosol|cytosol]] of the cell. The word glycolysis is of Greek origin, where &#039;glykos&#039; means sweet, and &#039;lysis&#039; means splitting. Hence, Glycolysis literally means &amp;quot;sugar splitting&amp;quot; or &amp;quot;sugar breaking&amp;quot;; this accurately describes the process of glycolysis, in which a 6-carbon sugar [[Molecule|molecule]] is broken down into two 3-carbon molecules. There are three stages in glycolysis which are [[Investment stage]], [[Splitting stage]] and [[Energy Yielding]] stage. Glycolysis consists of ten separate reactions, each catalysed by a different [[Enzyme|enzyme]]. Glycolysis is regulated by three different control enzymes. The first of these enzymes is [[Hexokinase|hexokinase]] which [[Phosphorylation|phosphorylates]] [[Glucose|glucose]], turning it into [[Glucose-6-phosphate|glucose-6-phosphate]]. The phosphorylated form of glucose is incapable of leaving the cell through the GLUT uniport transporter proteins in the cell membrane. The second is [[Phosphofructokinase|phosphofructokinase]]. This enzyme allows the production [[Fructose-1,6-bisphosphate|fructose-1,6-bisphosphate]] and is the rate-limiting step. The final control enzyme is [[Pyruvate kinase|pyruvate kinase]] which controls the rate of production of [[Pyruvate|pyruvate]], which is the final product of glycolysis. For each [[Molecule|molecule]] of [[Glucose|glucose]] that goes through the process of glycolysis, there is a net gain of 2 [[ATP|ATP]] molecules, 2 [[NADH|NADH]] [[Molecule|molecules]] and 2 [[Water|water molecules]] The pyruvate converted from glucose in Glycolysis then enters into the [[Citrate Acid Cycle]] which takes place in the [[Mitochondria]]&amp;lt;ref&amp;gt;Berg J., Tymoczko J and Stryer L. (2007) Biochemistry, 6th edition, New York, W. H. Freeman&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;Alberts et al., 2008, Molecular Biology of the Cell, 5th edition, pg 88-91, Garland Science, New York.&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
Under [[Anaerobic|anaerobic]] conditions, glycolysis is the only source of ATP. [[ATP|ATP]] is generated from [[ADP|ADP and]] an inorganic phosphate due to enough free energy being generated from the [[Oxidation|oxidation]] of glyceraldehyde-3-phosphate to 3-phosphoglycerate (an aldehyde to a carboxylic acid)&amp;lt;ref&amp;gt;Alberts et al., 2015, Molecular Biology of the Cell, 6th edition, pg 76-77, Garland Science, New York.&amp;lt;/ref&amp;gt;. The concentration of [[NAD+|NAD&amp;lt;sup&amp;gt;+&amp;lt;/sup&amp;gt;]] in the cytosol is not high, and it must therefore be regenerated from [[NADH|NADH]] in order for [[Glycolysis|glycolysis]] to continue. Under aerobic conditions, the hydrogen is transferred from NADH to one of several carriers that deliver it to the [[Respiratory chain|respiratory chain]] in the [[Mitochondria|mitochondria]], and ultimately to [[Oxygen|oxygen]]. Under anaerobic conditions, this is impossible; therefore, other means for [[Hydrogen|hydrogen]] disposal are required. [[Pyruvate|Pyruvate]] therefore acts as a hydrogen acceptor and is reduced to [[Lactate|lactate]] by [[Lactate dehydrogenase|lactate dehydrogenase]]. The lactate is released into the bloodstream, where it accumulates; it is removed and recycled after the restoration of oxygen supply. The muscle pain caused by lactate accumulation forces us to discontinue anaerobic exercise after a short while. In plants and some other microorganisms such as [[Yeast|yeast]], instead of lactate, [[Carbon dioxide|carbon dioxide]] and [[Ethanol|ethanol]] are produced to continue the regeneration of NAD&amp;lt;sup&amp;gt;+&amp;lt;/sup&amp;gt; and thus still supplying minimal ATP. &lt;br /&gt;
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=== References  ===&lt;br /&gt;
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&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Substrate&amp;diff=23700</id>
		<title>Substrate</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Substrate&amp;diff=23700"/>
		<updated>2018-12-17T13:23:16Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;This is the term referred to a [[Molecule|molecule]] which an [[Enzyme|enzyme]] interacts on to form an [[Enzyme-sustrate complex|enzyme-substrate complex]], through a [[Lock and key mechanism|lock and key mechanism]] or [[Induced fit mechanism|induced fit mechanism]]. This then causes a change in the structure of the enzyme by binding or cleaving parts. The substrate is then released from the enzyme as a [[Product|product]]&amp;lt;ref&amp;gt;Alberts B, Johnson A, Lewis J, Raff M, Roberts K, Walter P.  Molecular Biology of the Cell, 5th ed.  New York. Garland Science. 2008&amp;lt;/ref&amp;gt;. &lt;br /&gt;
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=== References  ===&lt;br /&gt;
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&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Valine&amp;diff=23699</id>
		<title>Valine</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Valine&amp;diff=23699"/>
		<updated>2018-12-17T13:22:58Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:Valine.png|right|Valine.png]] &lt;br /&gt;
&lt;br /&gt;
Valine is an [[Amino acid|amino acid]] with a large non-polar side chain -CH(CH&amp;lt;sub&amp;gt;3&amp;lt;/sub&amp;gt;)&amp;lt;sub&amp;gt;2 &amp;lt;/sub&amp;gt;&amp;lt;ref&amp;gt;Alberts, Bray, Hopkin, Johnson, Lewis, Raff, Roberts, Walter, 2010, Essential Cell Biology, Third Edition, New York, Garland Science&amp;lt;/ref&amp;gt;., with the three-letter code Val and the single letter code V. It is a hydrophobic amino acid. The [[Codon|codons]] for valine are GUU, GUC, GUA and GUG&amp;lt;ref&amp;gt;Berg, Tymoczko, Stryer (2007) Biochemistry, 6th Edition, New York: W.H. Freeman and Company.&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;Berg, J. M., Tymoczko, J. L., and Stryer, L. (2002). Biochemistry (5th ed.). New York: W.H. Freeman.&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Teichoic_acids&amp;diff=23698</id>
		<title>Teichoic acids</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Teichoic_acids&amp;diff=23698"/>
		<updated>2018-12-17T13:20:17Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;Teichoic acids are [[Polymer|polymers]] of [[Glycerol|glycerol]] or [[Ribitol|ribitol]] joined by [[Phosphates|phosphates]] and are found in the [[Cell wall|cell walls]] of [[Gram-positive bacteria|gram-positive bacteria]]&amp;lt;ref&amp;gt;J M. Willey, L M. Sherwood, C J. Woolverton. Prescott, Harley, and Klein’s Microbiology. 7th Ed, New York : The McGraw-Hill Companies. 2008.&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
Teichoic acids consist of [[Lipoteichoic acid|lipoteichoic acids]] (LTAs) and wall teichoic acids (WTAs). WTAs enable the [[Bacteria|bacterial]] cell to bind to [[Metal cations|metal cations]] outside the cell, such as&amp;amp;nbsp;[[Calcium|Ca&amp;lt;sup&amp;gt;2+&amp;lt;/sup&amp;gt;]]. This is said to affect the repulsion between neighbouring [[Phosphate groups|phosphate groups]] by decreasing the negative charge repulsion caused by the negatively charged [[Oxygen|oxygen]] present. By doing so, the WTAs alter the cell walls integrity without influencing the [[PH|pH]] gradient in the cell wall&amp;lt;ref&amp;gt;S Brown, J P. S Maria Jr., and S Walker. Wall Teichoic Acids of Gram-Positive Bacteria. Annual Review of Microbiology. 2013; 67: 313-336.&amp;lt;/ref&amp;gt;. Another metal cation they can bind to is Mg&amp;lt;sup&amp;gt;2+&amp;lt;/sup&amp;gt;, this is an important ion for bacterial cells as they aid in the synthesis of [[Peptidoglycan|peptidoglycan]] so are vital in the protection and maintenance of the bacterium&amp;lt;ref&amp;gt;Thomas KJ III, Rice CV. Revised Model of Calcium and Magnesium Binding to the Bacterial Cell Wall. 2014 [cited 25/11/18]; Available from:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4299761/&amp;lt;/ref&amp;gt;.&amp;lt;sup&amp;gt;&amp;lt;/sup&amp;gt; &lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Vena_cava&amp;diff=23697</id>
		<title>Vena cava</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Vena_cava&amp;diff=23697"/>
		<updated>2018-12-17T13:19:46Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;The vena cava is split into two structures the superior and the inferior vena cava, forming part of the [[Cardiovascular system|cardiovascular system]], being the two largest veins in the human body&amp;lt;ref&amp;gt;ThoughtCo. Regina Bailey. Superior and Inferior Venae Cavae. 2018 [Cited 06/12/18] Available from: https://www.thoughtco.com/venae-cavae-anatomy-373253&amp;lt;/ref&amp;gt;. The veins are a key component in the pulmonary circulatory system passing [[Deoxygenated blood|deoxygenated blood]] into the right [[Atrium|atrium]] of the heart from the rest of the body tissues, this allows the blood to then be passed via the hearts double circulatory system into the lungs to be re-oxygenated finally then is pumped through the aorta to the body tissues again allowing continual supply of oxygen to the muscles and cells to meet demand. &lt;br /&gt;
&lt;br /&gt;
The superior vena cava, also known as the anterior vena cava, passes deoxygenated blood to the right atrium from the upper cheat regions; head, neck and upper limbs. Positioned beside the aorta and pulmonary artery in the heart structure&amp;lt;ref&amp;gt;ThoughtCo. Regina Bailey. Superior and Inferior Venae Cavae. 2018 [Cited 06/12/18] Available from: https://www.thoughtco.com/venae-cavae-anatomy-373253&amp;lt;/ref&amp;gt;. It is formed from the connected brachiocephalic veins, which are positioned either side of the neck, and the azygos vein, which transports deoxygenated blood from the rib cage as it runs up the side of the thoracic vertebral column&amp;lt;ref&amp;gt;healthline. Brachiocephalic vein. 2015 [Cited 06/12/18] Available from: https://www.healthline.com/human-body-maps/brachiocephalic-vein#1&amp;lt;/ref&amp;gt;. The azygos vein is connected to both the superior and the inferior vena cava, and this allows an alternate route if there is a blockage in one the veins&amp;lt;ref&amp;gt;healthline. Brachiocephalic vein. 2015 [Cited 06/12/18] Available from: https://www.healthline.com/human-body-maps/brachiocephalic-vein#1&amp;lt;/ref&amp;gt;, allowing continuation in the flow of the circulatory system but at a lower efficiency. &lt;br /&gt;
&lt;br /&gt;
The inferior vena cava also referred to as the posterior vena cava, transports deoxygenated blood from the lower and middle regions of the body to the posterior region of the right atrium in the heart. The vein is positioned alongside the spine and travels in parallel to the descending aortic vessel&amp;lt;ref&amp;gt;ThoughtCo. Regina Bailey. Superior and Inferior Venae Cavae. 2018 [Cited 06/12/18] Available from: https://www.thoughtco.com/venae-cavae-anatomy-373253&amp;lt;/ref&amp;gt;. It is formed from the connection of the two common iliac veins; the internal iliac vein connects the blood supply from the visceral organs, and the external iliac vein transports the deoxygenated blood from the femoral veins in the legs&amp;lt;ref&amp;gt;healthlineRED. Common iliac vein. 2015 [Cited 06/12/18] Available from: https://www.healthline.com/human-body-maps/common-iliac-vein#1&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
=== Structure  ===&lt;br /&gt;
&lt;br /&gt;
The vena cava have walls comprised of three tissue layers which are characteristic to both arteries and veins; tunica initima, tunica media and tunica externa. The tunica initima is the thinnest and innermost layer, forming the endothelium lining – endothelial cells – which secretes molecules that lead to the promotion of smooth blood flow. Tunica media is the smooth muscle layer also composed of elastic fibres, but at a lower concentration than in the arteries, and connective tissues, all structured in a circular manner around the vessel&amp;lt;ref&amp;gt;lumencandela. Cardiovascular System: Blood Vessels. Blood Vessel Structure and Function. [Cited 06/12/18] Available from: https://courses.lumenlearning.com/boundless-ap/chapter/blood-vessel-structure-and-function/&amp;lt;/ref&amp;gt;., this layer forms a connection between the blood vessel and the nervous system&amp;lt;ref&amp;gt;ThoughtCo. Regina Bailey. Superior and Inferior Venae Cavae. 2018 [Cited 06/12/18] Available from: https://www.thoughtco.com/venae-cavae-anatomy-373253&amp;lt;/ref&amp;gt;. The outer layer tunica externa is formed primarily of [[Collagen|collagen]]&amp;lt;ref&amp;gt;ThoughtCo. Regina Bailey. Superior and Inferior Venae Cavae. 2018 [Cited 06/12/18] Available from: https://www.thoughtco.com/venae-cavae-anatomy-373253&amp;lt;/ref&amp;gt;. and connective fibres with an elastic lamina on the outside of the vessel, which is thicker in veins in comparison to arteries, this plays a key function in attaching the vein to the surrounding tissues; anchoring the vein in place is vital to ensure protection, especially to the superficial veins, and to prevent the structures collapsing&amp;lt;ref&amp;gt;lumencandela. Cardiovascular System: Blood Vessels. Blood Vessel Structure and Function. [Cited 06/12/18] Available from: https://courses.lumenlearning.com/boundless-ap/chapter/blood-vessel-structure-and-function/&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Vena_cava&amp;diff=23696</id>
		<title>Vena cava</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Vena_cava&amp;diff=23696"/>
		<updated>2018-12-17T13:19:26Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;The vena cava is split into two structures the superior and the inferior vena cava, forming part of the [[Cardiovascular system|cardiovascular system]], being the two largest veins in the human body&amp;lt;ref&amp;gt;ThoughtCo. Regina Bailey. Superior and Inferior Venae Cavae. 2018 [Cited 06/12/18] Available from: https://www.thoughtco.com/venae-cavae-anatomy-373253&amp;lt;/ref&amp;gt;. The veins are a key component in the pulmonary circulatory system passing [[Deoxygenated blood|deoxygenated blood]] into the right [[Atrium|atrium]] of the heart from the rest of the body tissues, this allows the blood to then be passed via the hearts double circulatory system into the lungs to be re-oxygenated finally then is pumped through the aorta to the body tissues again allowing continual supply of oxygen to the muscles and cells to meet demand. &lt;br /&gt;
&lt;br /&gt;
The superior vena cava, also known as the anterior vena cava, passes deoxygenated blood to the right atrium from the upper cheat regions; head, neck and upper limbs. Positioned beside the aorta and pulmonary artery in the heart structure&amp;lt;ref&amp;gt;ThoughtCo. Regina Bailey. Superior and Inferior Venae Cavae. 2018 [Cited 06/12/18] Available from: https://www.thoughtco.com/venae-cavae-anatomy-373253&amp;lt;/ref&amp;gt;. It is formed from the connected brachiocephalic veins, which are positioned either side of the neck, and the azygos vein, which transports deoxygenated blood from the rib cage as it runs up the side of the thoracic vertebral column&amp;lt;ref&amp;gt;healthline. Brachiocephalic vein. 2015 [Cited 06/12/18] Available from: https://www.healthline.com/human-body-maps/brachiocephalic-vein#1&amp;lt;/ref&amp;gt;. The azygos vein is connected to both the superior and the inferior vena cava, and this allows an alternate route if there is a blockage in one the veins&amp;lt;ref&amp;gt;healthline. Brachiocephalic vein. 2015 [Cited 06/12/18] Available from: https://www.healthline.com/human-body-maps/brachiocephalic-vein#1&amp;lt;/ref&amp;gt;., allowing continuation in the flow of the circulatory system but at a lower efficiency. &lt;br /&gt;
&lt;br /&gt;
The inferior vena cava also referred to as the posterior vena cava, transports deoxygenated blood from the lower and middle regions of the body to the posterior region of the right atrium in the heart. The vein is positioned alongside the spine and travels in parallel to the descending aortic vessel&amp;lt;ref&amp;gt;ThoughtCo. Regina Bailey. Superior and Inferior Venae Cavae. 2018 [Cited 06/12/18] Available from: https://www.thoughtco.com/venae-cavae-anatomy-373253&amp;lt;/ref&amp;gt;. It is formed from the connection of the two common iliac veins; the internal iliac vein connects the blood supply from the visceral organs, and the external iliac vein transports the deoxygenated blood from the femoral veins in the legs&amp;lt;ref&amp;gt;healthlineRED. Common iliac vein. 2015 [Cited 06/12/18] Available from: https://www.healthline.com/human-body-maps/common-iliac-vein#1&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
=== Structure ===&lt;br /&gt;
&lt;br /&gt;
The vena cava have walls comprised of three tissue layers which are characteristic to both arteries and veins; tunica initima, tunica media and tunica externa. The tunica initima is the thinnest and innermost layer, forming the endothelium lining – endothelial cells – which secretes molecules that lead to the promotion of smooth blood flow. Tunica media is the smooth muscle layer also composed of elastic fibres, but at a lower concentration than in the arteries, and connective tissues, all structured in a circular manner around the vessel&amp;lt;ref&amp;gt;lumencandela. Cardiovascular System: Blood Vessels. Blood Vessel Structure and Function. [Cited 06/12/18] Available from: https://courses.lumenlearning.com/boundless-ap/chapter/blood-vessel-structure-and-function/&amp;lt;/ref&amp;gt;., this layer forms a connection between the blood vessel and the nervous system&amp;lt;ref&amp;gt;ThoughtCo. Regina Bailey. Superior and Inferior Venae Cavae. 2018 [Cited 06/12/18] Available from: https://www.thoughtco.com/venae-cavae-anatomy-373253&amp;lt;/ref&amp;gt;. The outer layer tunica externa is formed primarily of [[Collagen|collagen]]&amp;lt;ref&amp;gt;ThoughtCo. Regina Bailey. Superior and Inferior Venae Cavae. 2018 [Cited 06/12/18] Available from: https://www.thoughtco.com/venae-cavae-anatomy-373253&amp;lt;/ref&amp;gt;. and connective fibres with an elastic lamina on the outside of the vessel, which is thicker in veins in comparison to arteries, this plays a key function in attaching the vein to the surrounding tissues; anchoring the vein in place is vital to ensure protection, especially to the superficial veins, and to prevent the structures collapsing&amp;lt;ref&amp;gt;lumencandela. Cardiovascular System: Blood Vessels. Blood Vessel Structure and Function. [Cited 06/12/18] Available from: https://courses.lumenlearning.com/boundless-ap/chapter/blood-vessel-structure-and-function/&amp;lt;/ref&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
=== References ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Pi-bonding&amp;diff=23695</id>
		<title>Pi-bonding</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Pi-bonding&amp;diff=23695"/>
		<updated>2018-12-17T13:17:41Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;A Pi-bond is a type of [[Covalent bond|covalent bond]] that is composed of the sideways overlap of two neighbouring P orbitals&amp;lt;ref&amp;gt;Chegg Study, Sigma and Pi Bonds https://www.chegg.com/homework-help/definitions/sigma-and-pi-bonds-6&amp;lt;/ref&amp;gt;. P orbitals have a dumb-bell shape and when they overlap to form a Pi-bond the structure consists of one P orbital above the molecular axis and one P orbital below the molecular axis. The Pi-bond is formed from unbound P-orbitals from neighbouring [[Atom|atoms]]. The Pi- bond is arranged from an unbound [[Electron|electron]] in the P-orbital of one atom bonding to an unbound electron in the P-orbital of another atom causing the P-orbitals to overlap sideways to form the Pi-bond. A [[Single bond|single bond]] is built up of one [[Sigma bonding|sigma bond]] and no Pi-bonds whereas a [[Double bond|double bond]] is build up of a sigma bond and a Pi-bond&amp;lt;ref&amp;gt;Helmenstine, Anne Marie, Ph.D. &amp;quot;Pi Bond Definition in Chemistry.&amp;quot; ThoughtCo, Dec. 5, 2018, thoughtco.com/definition-of-pi-bond-605519.&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;http://www.chem.ucla.edu/~harding/IGOC/P/pi_bond.html&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
See [[Orbitals|Orbitals]] &lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Pi-bonding&amp;diff=23694</id>
		<title>Pi-bonding</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Pi-bonding&amp;diff=23694"/>
		<updated>2018-12-17T13:17:24Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;span style=&amp;quot;font-size: 13.28px;&amp;quot;&amp;gt;A Pi-bond is a type of &amp;lt;/span&amp;gt;[[Covalent bond|covalent bond]]&amp;lt;span style=&amp;quot;font-size: 13.28px;&amp;quot;&amp;gt; that is composed of the sideways overlap of two neighbouring P orbitals&amp;lt;/span&amp;gt;&amp;lt;ref&amp;gt;Chegg Study, Sigma and Pi BondsfckLRhttps://www.chegg.com/homework-help/definitions/sigma-and-pi-bonds-6&amp;lt;/ref&amp;gt;&amp;lt;span style=&amp;quot;font-size: 13.28px;&amp;quot;&amp;gt;. P orbitals have a dumb-bell shape and when they overlap to form a Pi-bond the structure consists of one P orbital above the molecular axis and one P orbital below the molecular axis. The Pi-bond is formed from unbound P-orbitals from neighbouring &amp;lt;/span&amp;gt;[[Atom|atoms]]&amp;lt;span style=&amp;quot;font-size: 13.28px;&amp;quot;&amp;gt;. The Pi- bond is arranged from an unbound &amp;lt;/span&amp;gt;[[Electron|electron]]&amp;lt;span style=&amp;quot;font-size: 13.28px;&amp;quot;&amp;gt; in the P-orbital of one atom bonding to an unbound electron in the P-orbital of another atom causing the P-orbitals to overlap sideways to form the Pi-bond. A &amp;lt;/span&amp;gt;[[Single bond|single bond]]&amp;lt;span style=&amp;quot;font-size: 13.28px;&amp;quot;&amp;gt; is built up of one &amp;lt;/span&amp;gt;[[Sigma bonding|sigma bond]]&amp;lt;span style=&amp;quot;font-size: 13.28px;&amp;quot;&amp;gt; and no Pi-bonds whereas a &amp;lt;/span&amp;gt;[[Double bond|double bond]]&amp;lt;span style=&amp;quot;font-size: 13.28px;&amp;quot;&amp;gt; is build up of a sigma bond and a Pi-bond&amp;lt;/span&amp;gt;&amp;lt;ref&amp;gt;Helmenstine, Anne Marie, Ph.D. &amp;quot;Pi Bond Definition in Chemistry.&amp;quot; ThoughtCo, Dec. 5, 2018, thoughtco.com/definition-of-pi-bond-605519.&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;http://www.chem.ucla.edu/~harding/IGOC/P/pi_bond.html&amp;lt;/ref&amp;gt;&amp;lt;span style=&amp;quot;font-size: 13.28px;&amp;quot;&amp;gt;.&amp;lt;/span&amp;gt;&lt;br /&gt;
&lt;br /&gt;
See [[Orbitals|Orbitals]] &lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt; &lt;br /&gt;
&lt;br /&gt;
&amp;lt;br&amp;gt; &lt;br /&gt;
&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Pi-bonding&amp;diff=23693</id>
		<title>Pi-bonding</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Pi-bonding&amp;diff=23693"/>
		<updated>2018-12-17T13:16:46Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:Pi bond01.png|right|50%x50%px|50%x50%px]] &lt;br /&gt;
&lt;br /&gt;
A Pi-bond is a type of [[Covalent bond|covalent bond]] that is composed of the sideways overlap of two neighbouring P orbitals&amp;lt;ref&amp;gt;Chegg Study, Sigma and Pi BondsfckLRhttps://www.chegg.com/homework-help/definitions/sigma-and-pi-bonds-6&amp;lt;/ref&amp;gt;. P orbitals have a dumb-bell shape and when they overlap to form a Pi-bond the structure consists of one P orbital above the molecular axis and one P orbital below the molecular axis. The Pi-bond is formed from unbound P-orbitals from neighbouring [[Atom|atoms]]. The Pi- bond is arranged from an unbound [[Electron|electron]] in the P-orbital of one atom bonding to an unbound electron in the P-orbital of another atom causing the P-orbitals to overlap sideways to form the Pi-bond. A [[Single bond|single bond]] is built up of one [[Sigma bonding|sigma bond]] and no Pi-bonds whereas a [[Double bond|double bond]] is build up of a sigma bond and a Pi-bond&amp;lt;ref&amp;gt;Helmenstine, Anne Marie, Ph.D. &amp;quot;Pi Bond Definition in Chemistry.&amp;quot; ThoughtCo, Dec. 5, 2018, thoughtco.com/definition-of-pi-bond-605519.&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;http://www.chem.ucla.edu/~harding/IGOC/P/pi_bond.html&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
See [[Orbitals|Orbitals]]&lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt; &lt;br /&gt;
&lt;br /&gt;
&amp;lt;br&amp;gt; &lt;br /&gt;
&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Energy&amp;diff=23692</id>
		<title>Energy</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Energy&amp;diff=23692"/>
		<updated>2018-12-17T13:14:38Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;It is something that an object needs to do work. The standard unit of energy is the [[Joule|Joule]] (J) which is defined as the energy exerted on an object by a force of one [[Newton|Newton]] over a distance of one [[metre|metre]]. The first law of [[Thermodynamics|Thermodynamics]] states that energy cannot be created nor destroyed and is instead transformed from one form to another&amp;lt;ref&amp;gt;Encyclopædia Britannica. Energy Conversion. 2016 [cited 23/10/17]; Available from: https://www.britannica.com/technology/energy-conversion&amp;lt;/ref&amp;gt;. Energy can be caluclated through the equation E= mc&amp;lt;sup&amp;gt;2&amp;amp;nbsp; &amp;lt;/sup&amp;gt;where m is the [[mass|mass]] of an object and c the [[speed of light|speed of light]] within a [[vacuum|vacuum]].&amp;lt;br&amp;gt; &lt;br /&gt;
&lt;br /&gt;
=== References ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Xenophagy&amp;diff=23691</id>
		<title>Xenophagy</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Xenophagy&amp;diff=23691"/>
		<updated>2018-12-17T13:12:59Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;Xenophagy is the process of [[Autophagy]] by which [[cytosolic|cytosolic]] or vacuole-dwelling [[pathogens|pathogens]] are degraded&amp;lt;ref&amp;gt;Leigh A. Knodler and Jean Celli. Eating the strangers within: host control of intracellular bacteria via xenophagy. Cell Microbiol. 2011. 9, 1319-1327&amp;lt;/ref&amp;gt;. These pathogens are recognised non-specifically by their [[lipopolysaccharide|lipopolysaccharide]] or [[peptidoglycan|peptidoglycan]] outer layers and are resultantly engulphed into autophagosomes (double-membraned organelles)&amp;lt;ref&amp;gt;Leigh A. Knodler and Jean Celli. Eating the strangers within: host control of intracellular bacteria via xenophagy. Cell Microbiol. 2011. 9, 1319-1327&amp;lt;/ref&amp;gt;. This autophagosome migrates to and fuses with a [[lysosome|lysosome]], releasing its contents into the lysosome where they are then hydrolysed by degradative [[enzymes|enzymes]]&amp;lt;ref&amp;gt;Cell Research: Yuchen Feng, Ding He, Zhiyuan Yao &amp;amp;amp;amp;amp; Daniel J Klionsky: The machinery of macroautophagy: 2013 [cited 20/11/2018]  Available from: https://www.nature.com/articles/cr2013168#abstract&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
Xenophagy plays a key role in [[innate immunity|innate immunity]] - pathogens can be recognised by general pathogenic characteristics and destroyed before they cause infection in cells, thus an immune response is not required&amp;lt;ref&amp;gt;Leigh A. Knodler and Jean Celli. Eating the strangers within: host control of intracellular bacteria via xenophagy. Cell Microbiol. 2011. 9, 1319-1327&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
=== References ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Radioactive&amp;diff=23690</id>
		<title>Radioactive</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Radioactive&amp;diff=23690"/>
		<updated>2018-12-14T15:15:21Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;An [[Atom|atom]] is said to be radioactive if it randomly emits radiation in one of three forms; [[Alpha particle|alpha particles]], [[Beta particle|beta particles]] and [[Gamma rays|gamma rays]]&amp;lt;ref&amp;gt;What is nuclear (2016) can be found at https://whatisnuclear.com/articles/radioactivity.html assessed: 21/10/2016&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Nonsense_mutation&amp;diff=23689</id>
		<title>Nonsense mutation</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Nonsense_mutation&amp;diff=23689"/>
		<updated>2018-12-10T20:18:47Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;Nonsense mutation is when there is a [[Nucleotide|nucleotide]] substitution causing a different [[Amino acid|amino acid]] to be coded for, which creates a&amp;amp;nbsp;[[Stop codon|stop codon]]&amp;amp;nbsp;. This causes the protein that is being encoded for to be truncated due to the premature termination of [[Translation|translation]]&amp;lt;ref&amp;gt;Hartl, D. and Jones, E. (2009) Genetics: Genes and Genomes, U.S.A: Jones and Bartlett, page 515&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Nonsense_mutation&amp;diff=23688</id>
		<title>Nonsense mutation</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Nonsense_mutation&amp;diff=23688"/>
		<updated>2018-12-10T20:18:26Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;Nonsense mutation is when there is a [[nucleotide|nucleotide]] substitution causing a different [[Amino acid|amino acid]] to be coded for, which creates a&amp;amp;nbsp;[[Stop codon|stop codon]]&amp;amp;nbsp;. This causes the protein that is being encoded for to be truncated due to the premature termination of [[Translation|translation&amp;lt;ref&amp;gt;Hartl, D. and Jones, E. (2009) Genetics: Genes and Genomes, U.S.A: Jones and Bartlett, page 515&amp;lt;/ref&amp;gt;]]. &lt;br /&gt;
&lt;br /&gt;
&amp;lt;sup&amp;gt;&amp;lt;/sup&amp;gt; &lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&amp;lt;br&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;amp;nbsp;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Stimulus&amp;diff=23687</id>
		<title>Stimulus</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Stimulus&amp;diff=23687"/>
		<updated>2018-12-10T20:16:54Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;A stimulus is a noticeable change in the internal or external [[Environment|environment]]. This provokes a response within an [[Organism|organism]]. A stimulus may not only be physiological, but also psychological, whereby an action of another individual directly affects the [[Behaviour|behaviour]] of another. &lt;br /&gt;
&lt;br /&gt;
=== Types of receptors in the human body  ===&lt;br /&gt;
&lt;br /&gt;
[[Chemoreceptors|Chemoreceptors]], detect the presence of chemicals. [[Thermoreceptors|Thermoreceptors]], on the other hand, detect changes in temperature. [[Mechanoreceptors|Mechanoreceptors]] detect mechanical forces. [[Photoreceptors|Photoreceptors]] in the body, detect light during vision&amp;lt;ref&amp;gt;Sensory Receptors | Boundless Anatomy and Physiology [Internet]. Courses.lumenlearning.com. 2018 [cited 10 December 2018]. Available from: https://courses.lumenlearning.com/boundless-ap/chapter/sensory-receptors/&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Basal_bodies&amp;diff=23686</id>
		<title>Basal bodies</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Basal_bodies&amp;diff=23686"/>
		<updated>2018-12-10T20:15:24Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;Basal Bodies&amp;amp;nbsp;are small complex structures embedded in [[cell|cell]] surface to which [[flagella|flagella]] hook is connected&amp;lt;ref&amp;gt;Neidhardt FC, Ingraham JL, Schaechter M. Physiology of the Bacterial Cell: A Molecular Approach. Massachusetts: Sinauer Associates. 1990.&amp;lt;/ref&amp;gt;.&amp;amp;nbsp;The basal bodies of the [[Gram-positive|Gram-positive]] and [[Gram-negative|Gram-negative]] [[bacteria|bacteria]] vary due to the difference in their outer envelope stuctures. They contain 15 or more [[proteins|proteins]] that cluster together to form a rod to which 4 rings are attached in Gram-negative bacteria and 2 rings in Gram-positive bacteria&amp;lt;ref&amp;gt;Neidhardt FC, Ingraham JL, Schaechter M. Physiology of the Bacterial Cell: A Molecular Approach. Massachusetts: Sinauer Associates. 1990.&amp;lt;/ref&amp;gt;.&amp;lt;br&amp;gt; &lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=16S_rRNA&amp;diff=23685</id>
		<title>16S rRNA</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=16S_rRNA&amp;diff=23685"/>
		<updated>2018-12-10T20:14:22Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:16s rna.gif|right|16s rna.gif]] 16S rRNA is found within the 30S [[RRNA|rRNA]] sub-unit of ribosomes. 16S rRNA contains a ribosomal binding site, known as the [[Shine dalgarno|Shine Dalgarno]] sequence. During translation of [[Protein synthesis|protein synthesis]], the initiator region of [[MRNA|mRNA]] binds very near the 3&#039; end of the 16S rRNA at the [[Shine dalgarno|Shine Dalgarno]] sequence. The number of base pairs linking mRNA and 16S rRNA ranges from three to nine&amp;lt;ref&amp;gt;Alberts, B et al. (2008) The Molecular Biology of the Cell, 5th Ed., New York: Garland Science, Taylor and Francis Group, LLC.&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;16S RNA Structure [Internet]. Use of 16S rRNA and rpoB Genes as Molecular Markers for Microbial Ecology Studies. American Society for Microbiology Journals; 2006 [cited 2018Dec10]. Available from: https://aem.asm.org/content/73/1/278/figures-only&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=16S_rRNA&amp;diff=23684</id>
		<title>16S rRNA</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=16S_rRNA&amp;diff=23684"/>
		<updated>2018-12-10T20:14:00Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:16s rna.gif|right|16s rna.gif]]&amp;lt;ref&amp;gt;16S RNA Structure [Internet]. Use of 16S rRNA and rpoB Genes as Molecular Markers for Microbial Ecology Studies. American Society for Microbiology Journals; 2006 [cited 2018Dec10]. Available from: https://aem.asm.org/content/73/1/278/figures-only&amp;lt;/ref&amp;gt;. 16S rRNA is found within the 30S [[RRNA|rRNA]] sub-unit of ribosomes. 16S rRNA contains a ribosomal binding site, known as the [[Shine dalgarno|Shine Dalgarno]] sequence. During translation of [[Protein synthesis|protein synthesis]], the initiator region of [[MRNA|mRNA]] binds very near the 3&#039; end of the 16S rRNA at the [[Shine dalgarno|Shine Dalgarno]] sequence. The number of base pairs linking mRNA and 16S rRNA ranges from three to nine&amp;lt;ref&amp;gt;Alberts, B et al. (2008) The Molecular Biology of the Cell, 5th Ed., New York: Garland Science, Taylor and Francis Group, LLC.&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=16S_rRNA&amp;diff=23683</id>
		<title>16S rRNA</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=16S_rRNA&amp;diff=23683"/>
		<updated>2018-12-10T20:13:45Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:16s rna.gif|right]]&amp;lt;ref&amp;gt;16S RNA Structure [Internet]. Use of 16S rRNA and rpoB Genes as Molecular Markers for Microbial Ecology Studies. American Society for Microbiology Journals; 2006 [cited 2018Dec10]. Available from: https://aem.asm.org/content/73/1/278/figures-only&amp;lt;/ref&amp;gt;. 16S rRNA is found within the 30S [[RRNA|rRNA]] sub-unit of ribosomes. 16S rRNA contains a ribosomal binding site, known as the [[Shine dalgarno|Shine Dalgarno]] sequence. During translation of [[Protein synthesis|protein synthesis]], the initiator region of [[MRNA|mRNA]] binds very near the 3&#039; end of the 16S rRNA at the [[Shine dalgarno|Shine Dalgarno]] sequence. The number of base pairs linking mRNA and 16S rRNA ranges from three to nine&amp;lt;ref&amp;gt;Alberts, B et al. (2008) The Molecular Biology of the Cell, 5th Ed., New York: Garland Science, Taylor &amp;amp;amp;amp;amp;amp;amp;amp;amp; Francis Group, LLC.&amp;lt;/ref&amp;gt;.     &lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Blood_glucose_level&amp;diff=23682</id>
		<title>Blood glucose level</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Blood_glucose_level&amp;diff=23682"/>
		<updated>2018-12-10T20:13:05Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;Blood glucose level is the amount of sugar ([[Glucose|Glucose]]) in an individuals&#039; [[Blood stream|blood stream]] at any given time&amp;lt;ref name=&amp;quot;Diabetes UK Blood Glucose&amp;quot;&amp;gt;http://www.diabetes.co.uk/diabetes_care/Diabetes_and_blood_glucose.html&amp;lt;/ref&amp;gt;. Blood glucose levels can be measured using an appropriate test strip, a [[Blood glucose meter|blood glucose meter]] and a small needle to prick the patient&#039;s finger with&amp;lt;ref name=&amp;quot;Diabetes Care&amp;quot;&amp;gt;http://www.mylife-diabetescare.co.uk/mylife-diabetes-knowledge-correct-measurement.html&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
The normal range for a healthy patient without [[Diabetes|diabetes is]] between 4-8 mmol/L however the values for a diabetic patient will fluctuate more due to the problems with their [[Insulin|insulin]]&amp;lt;ref name=&amp;quot;Diabetes UK Blood Glucose Ranges&amp;quot;&amp;gt;http://www.diabetes.co.uk/diabetes_care/blood-sugar-level-ranges.html&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
People with diabetes are more susceptible to [[Hypoglycaemia|hypoglycaemia]] (which is low blood sugar) and [[Hyperglycaemia|hyperglycaemia]] (which is high blood glucose) which can cause detrimental effects to the body&amp;lt;ref&amp;gt;http://www.visionaware.org/info/your-eye-condition/diabetic-retinopathy/hyperglycemia-and-hypoglycemia/125&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
Hypoglycemia is caused usually due to an insulin overdose (common in type 1 diabetics), during or after intensive exercise, or during starvation. Hyperglycemia, however, is as a result of either insufficient insulin production (the issue for type 1 diabetics), insulin resistance (which is common in type 2 sufferers), or postprandial due to the consumption of food.&lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Kinase&amp;diff=23681</id>
		<title>Kinase</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Kinase&amp;diff=23681"/>
		<updated>2018-12-10T20:12:24Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;A kinase is an [[Enzyme|enzyme]] that catalyses the addition of [[Phosphate|phosphate groups]] ([[Phosphorylation|phosphorylation]]) to specific substrates using ATP, forming a [[Covalent bond|covalent bond]] with this [[Substrate|substrate]]&amp;lt;ref&amp;gt;Molecular biology of the cell (5th edition), Alberts et al. Garland Science, 2008&amp;lt;/ref&amp;gt;. There are currently 518 known protein kinase genes in the [[Human genome|human genome]]&amp;lt;ref name=&amp;quot;null&amp;quot;&amp;gt;Manning G, Whyte DB, Martinez R, Hunter T, Sudarsanam S (2002) The protein kinase complement of the human genome. Science 298: 1912-1934&amp;lt;/ref&amp;gt;. Furthermore, kinases are commonly found in [[Cell signalling pathways|cell signalling pathways]], where they will activate or deactivate [[Enzymes|enzymes]]. An example of cell signalling of this sort is when the [[Hormone|hormone]] [[Epinephrine|epinephrine]] is released and a series of kinases will activate the [[Phosphorylase A|phosphorylase A]] and deactivate [[Glycogen synthase|glycogen synthase]] A to aid in the [[Hydrolysis|hydrolysis]] of [[Glycogen|glycogen]] into [[Glucose|glucose]] to provide energy&amp;lt;ref&amp;gt;Berg JM, Tymoczko JL, Stryer L. Biochemistry. 5th edition. New York: W H Freeman; 2002. Section 21.3, Epinephrine and Glucagon Signal the Need for Glycogen Breakdown. Available from: https://www.ncbi.nlm.nih.gov/books/NBK22429/&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
=== Studying Kinase Activity  ===&lt;br /&gt;
&lt;br /&gt;
It is very difficult to perform enzyme reaction analysis due to the limited methods available alongside the fact that large protein catalysts are highly complex. Over the recent decades, many studies have been carried out in terms of the action of kinases, such as energy studies that measured the Bronsted nucleophile coefficient to aid in understanding the transition state. By substituting flurorine atoms on the phenol ring it was possible to study tyrosine kinase activity, this proved that phosphoryl transfer rate is almost indepent of the nucleophiole pKa&amp;lt;ref&amp;gt;Kim K, Cole PA. Measurement of a Brønsted nucleophile coefficient and insights into the transition state for a protein tyrosine kinase. Journal of the American Chemical Society. 1997;119:11096–11097&amp;lt;/ref&amp;gt;. It is possible to identify active states of kinases by crystallography using macroscopic and microscopic features required for phosphoryl transfer. This is due to the fact that a hydrophobic spine is created when N terminal and C terminal lobes interact which in turn interact with kinases&amp;lt;ref&amp;gt;Surface comparison of active and inactive protein kinases identifies a conserved activation mechanism. Kornev AP, Haste NM, Taylor SS, Eyck LF Proc Natl Acad Sci U S A. 2006 Nov 21; 103(47):17783-8.&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
=== Some Common Kinases ===&lt;br /&gt;
&lt;br /&gt;
*[[Protein kinase A|Protein Kinase A]] - involved in cAMP-Dependant phosphorylation cascade&lt;br /&gt;
*[[Protein Kinase C|Protein Kinase C]] - involved in Signal cascades which release DAG, IP3 and Calcium ions&lt;br /&gt;
*[[Glycogenolysis|Glycogen Phosphorylase Kinase]] - involved in regulation of blood glucose concentration by activating Glycogen phosphorylase which depolymerises Glycogen&lt;br /&gt;
*[[Cell cycle|Cyclin Dependant Kinases]] - involved in regulation of cell cycle and the progession between each phase&amp;lt;br&amp;gt;&lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Catalyst&amp;diff=23680</id>
		<title>Catalyst</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Catalyst&amp;diff=23680"/>
		<updated>2018-12-10T20:11:18Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;A catalyst is a substance that can be in a solid, liquid or gaseous form. The aim of a catalyst is to increase the [[Rate of reaction|rate of a reaction]] by lowering the activation [[Enthalpy|enthalpy]] of a [[Reaction|reaction]]. Meaning a higher majority of the [[Atoms|atoms]] or&amp;amp;nbsp;[[Molecules|molecules]] can react, so more product is formed from reactants. A catalyst itself is unchanged at the end of a reaction, therefore, can be reused&amp;lt;ref&amp;gt;Hamers L. Explainer: What is a catalyst? [Internet]. Science News for Students. 2018 [cited 10 December 2018]. Available from: https://www.sciencenewsforstudents.org/article/explainer-catalyst-chemistry&amp;lt;/ref&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
See [[Catalysis|Catalysis]]. &lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=2-methylpropane&amp;diff=23679</id>
		<title>2-methylpropane</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=2-methylpropane&amp;diff=23679"/>
		<updated>2018-12-10T20:10:16Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;2-methylpropane is an organic [[Compound|compound]] made up of [[Hydrogen|hydrogen]] and [[Carbon|carbon]]. Its carbon chain is 3 carbons long that are all attached to hydrogens and the second carbon along is attached to a [[methyl group|methyl group]]&amp;lt;ref&amp;gt;{{ https://pubchem.ncbi.nlm.nih.gov/compound/59915248  }}&amp;lt;/ref&amp;gt;. Also known as i-butane, occupying the chemical formula HC(CH&amp;lt;sub&amp;gt;3&amp;lt;/sub&amp;gt;)&amp;lt;sub&amp;gt;3&amp;lt;/sub&amp;gt;, is the simplest alkane with a tertiary carbon. I-butane is a precursor molecule in the petrochemical industry, such as the production of [[isooctane|isooctane]]. The production of isooctane is useful because it is used as a fuel. 2-methylpropane is useful to chemical engineers because not only is it used in chemical synthesis of useful fuels, but it has a relatively low vapour density (21 degrees Celcius) which means it can be stored easily and safely&amp;lt;ref&amp;gt;{{ https://www.sigmaaldrich.com/catalog/product/aldrich/295450}}&amp;lt;/ref&amp;gt;. On the contrary, 2-methylpropane should be handled with caution, such as eyeshields and gloves should be used. &lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Cervical_canal&amp;diff=23678</id>
		<title>Cervical canal</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Cervical_canal&amp;diff=23678"/>
		<updated>2018-12-10T20:08:25Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: Cleaned up the references.&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:Screenshot 2018-12-10 at 11.28.12.png|right|Screenshot 2018-12-10 at 11.28.12.png]] &lt;br /&gt;
&lt;br /&gt;
The uterus is made up of a body and a [[Cervix|cervix]]. The cervix communicates superiorly with the uterine cavity through the internal orifice (known as internal as a communicates inferiorly with the [[Vagina|vagina]] at the external orifice (known as the external os)&amp;lt;ref&amp;gt;Cervical Canal • Reproductive • AnatomyZone [Internet]. AnatomyZone. 2018 [cited 10 December 2018]. Available from: http://anatomyzone.com/anatomy-feed/cervical-canal/&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;Check S. [Internet]. Structure &amp;amp;amp;amp;amp;amp;amp;amp; Function. [cited 2018Dec10]. Available from: https://www.haad.ae/simplycheck/tabid/71/default.aspx&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
The cervical canal is the narrow passage which runs through the cervix, which is what connects the vagina to the [[Uterus|uterus]]. It is the lowermost part of the uterus and is consists of strong muscles. &lt;br /&gt;
&lt;br /&gt;
The cervix directs the [[Sperm|sperm]] to the uterus during sexual intercourse, as well as allowing the flow of menstrual blood from the uterus into the [[Vagina|vagina]]. &lt;br /&gt;
&lt;br /&gt;
The opening of the cervical canal is usually narrow, however, pressure from the fetal head as well as [[Hormones|hormones]] found in the body can cause this opening to widen to about 4 inches. To allow the birth of a baby, the opening widens as well&amp;lt;ref&amp;gt;Check S. [Internet]. Structure &amp;amp;amp;amp;amp;amp;amp;amp;amp; Function. [cited 2018Dec10]. Available from: https://www.haad.ae/simplycheck/tabid/71/default.aspx&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=MDNA&amp;diff=23677</id>
		<title>MDNA</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=MDNA&amp;diff=23677"/>
		<updated>2018-12-10T20:06:35Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;Mitochondrial DNA (sometimes called mtDNA or mDNA) is [[DNA synthesis|DNA]] that is found in the [[Mitochondria]]&amp;lt;ref&amp;gt;What is mitochondrial DNA? - Genetics Home Reference. 2015. What is mitochondrial DNA? - Genetics Home Reference. [ONLINE] Available at: http://ghr.nlm.nih.gov/handbook/basics/mtdna. [Accessed 20 October 2015].&amp;lt;/ref&amp;gt;. mDNA is usually inherited from the mother&amp;lt;ref&amp;gt;Mitochondrial inheritance. 2015. Mitochondrial inheritance. [ONLINE] Available at: http://www.geneticseducation.nhs.uk/genetic-glossary/212-mitochondrial-inheritance. [Accessed 20 October 2015].&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
Hereditary traits in [[Eukaryotes|Eukaryotes]] can be determined by [[Genes|genes]] in the DNA of the Mitochondria. In humans, the Mitochondrial DNA contains 37 genes which code for 13 [[Protein|protein]], 22 [[TRNA|tRNAs]] and 2 [[RRNA|rRNA]] molecules.&amp;lt;ref name=&amp;quot;[3]&amp;quot;&amp;gt;Hartl,DL and Jones,EW. 2009. Chapter 16 - Mitochondrial DNA and Extranuclear Inheritance. Genetics analysis of genes and genomes 7th Edition. Pg 588.&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;Anderson S, Bankier AT, Barrell BG, de Bruijn MHL, Coulson AR, Drouin J, Eperon IC, Nierlich DP, Roe BA, Sanger F, et al. Sequence and organization of the human mitochondrial genome. Nature. 1981;290(5806):457-465&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
Due to the function of Mitochondria, mutations of the MDNA can cause [[Neuromuscular disorders|neuromuscular disorders]]. However, mitochondrial conditions are not always caused by mutations in the MDNA but can be down to mutations of the genes in the [[Nucleus|Nucleus]] of the [[Cell|cell]] that determine Mitochondrial function&amp;lt;ref&amp;gt;Mitochondrial inheritance. 2015. Mitochondrial inheritance. [ONLINE] Available at: http://www.geneticseducation.nhs.uk/genetic-glossary/212-mitochondrial-inheritance. [Accessed 20 October 2015].&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=MDNA&amp;diff=23676</id>
		<title>MDNA</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=MDNA&amp;diff=23676"/>
		<updated>2018-12-10T20:06:15Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: Cleaned up the references.&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;Mitochondrial DNA (sometimes called mtDNA or mDNA) is [[DNA synthesis|DNA]] that is found in the [[Mitochondria]]&amp;lt;ref&amp;gt;What is mitochondrial DNA? - Genetics Home Reference. 2015. What is mitochondrial DNA? - Genetics Home Reference. [ONLINE] Available at: http://ghr.nlm.nih.gov/handbook/basics/mtdna. [Accessed 20 October 2015].&amp;lt;/ref&amp;gt;. mDNA is usually inherited from the mother&amp;lt;ref&amp;gt;Mitochondrial inheritance. 2015. Mitochondrial inheritance. [ONLINE] Available at: http://www.geneticseducation.nhs.uk/genetic-glossary/212-mitochondrial-inheritance. [Accessed 20 October 2015].&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
Hereditary traits in [[Eukaryotes|Eukaryotes]] can be determined by [[Genes|genes]] in the DNA of the Mitochondria. In humans, the Mitochondrial DNA contains 37 genes which code for 13 [[Protein|protein]], 22 [[TRNA|tRNAs]] and 2 [[RRNA|rRNA]] molecules.&amp;lt;ref name=&amp;quot;[3]&amp;quot;&amp;gt;Hartl,DL and Jones,EW. 2009. Chapter 16 - Mitochondrial DNA and Extranuclear Inheritance. Genetics analysis of genes and genomes 7th Edition. Pg 588.&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;Anderson S, Bankier AT, Barrell BG, de Bruijn MHL, Coulson AR, Drouin J, Eperon IC, Nierlich DP, Roe BA, Sanger F, et al. Sequence and organization of the human mitochondrial genome. Nature. 1981;290(5806):457-465&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
Due to the function of Mitochondria, mutations of the MDNA can cause [[Neuromuscular disorders|neuromuscular disorders]]. However, mitochondrial conditions are not always caused by mutations in the MDNA but can be down to mutations of the genes in the [[Nucleus|Nucleus]] of the [[Cell|cell]] that determine Mitochondrial function&amp;lt;ref&amp;gt;[2]&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Connective_tissue&amp;diff=23675</id>
		<title>Connective tissue</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Connective_tissue&amp;diff=23675"/>
		<updated>2018-12-10T20:05:15Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;Connective tissue is any supporting tissue in which cells are embedded in an [[Extra-cellular matrix|extra-cellular matrix]] (a network of [[Polysaccharides|polysaccharides]] and proteins- particularly [[Collagen|collagen]])&amp;lt;ref&amp;gt;Alberts, Johnson, Lewis, Raff, Roberts, Walter (2008). Molecular Biology of the Cell. 5th ed. New York: Garland Science Taylor and Francis Group. G9.&amp;lt;/ref&amp;gt;. It often lies between different tissues, connecting, supporting, binding to or separating them depending on specific location and function in a multi-cellular [[Organism|organism]]. &lt;br /&gt;
&lt;br /&gt;
Connective tissue can take many different structures; when calcified they become very hard like teeth or bone, then can form rope like structures with high mechanical strength forming [[Tendons|tendons]], they are also responsible for the colourless gel of the [[Cornea|cornea]] in the [[Eye|eye]]&amp;lt;ref&amp;gt;Alberts, Johnson, Lewis, Raff, Roberts, Walter (2008). Molecular Biology of the Cell. 5th ed. New York: Garland Science Taylor and Francis Group. p1178&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
Connective tissue is a structure in which cells adhere, to each other and to the extracellular matrix. This is necessary in multi-cellular organisms to provide mechanical strength but also to allow interaction, behaviour coordination, and regulation of [[Gene expression|gene expression]]&amp;lt;ref&amp;gt;Alberts, Johnson, Lewis, Raff, Roberts, Walter (2008). Molecular Biology of the Cell. 5th ed. New York: Garland Science Taylor and Francis Group. p1131&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
Connective tissue is made up of cells surrounded by large amounts of extracellular matrix which is predominantly secreted by [[Fibroblasts|fibroblasts]]. Connective tissue is rich in extracellular matrix and cells are sparsely dispersed within it. The extracellular matrix in these connective tissues influences survival, development, migration, rapid reproduction of cells, their shape, and function&amp;lt;ref&amp;gt;Alberts, Johnson, Lewis, Raff, Roberts, Walter (2008). Molecular Biology of the Cell. 5th ed. New York: Garland Science Taylor and Francis Group. p1178&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
An example of a specialised connective tissue is [[collagen|collagen]]. &lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Diploid_cell&amp;diff=23674</id>
		<title>Diploid cell</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Diploid_cell&amp;diff=23674"/>
		<updated>2018-12-10T20:04:42Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;Diploid cells, or somatic cells, contain two complete copies of each [[Chromosome|chromosome]] within the cell [[Nucleus|nucleus]]. The two copies of one [[Chromosome|chromosome]] pair up and are called [[Homologous chromosomes|homologous chromosomes]]. Human diploid cells consist of 46 chromosomes which include all cells, with the exception of [[Gametes|gamete cells]] containing half of the required genetic information and are referred to as [[Haploid]]. Any cell with homologous chromosomes is said to be [[Diploid|diploid]]. The diploid number of a [[Cell proliferation|cell]] is commonly abbreviated to 2n, where n is the number of chromosomes. Diploid cells are produced by [[Mitosis|mitosis]] and the [[Daughter cells|daughter cells]] are exact replicas of the [[Parent cell|parent cell]]. Examples of diploid cells include skin cells and [[Muscle cell|muscle cells]].&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Rate_of_reaction&amp;diff=23673</id>
		<title>Rate of reaction</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Rate_of_reaction&amp;diff=23673"/>
		<updated>2018-12-10T20:03:47Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;The rate of reaction is a measure of the speed at which the [[reactants|reactants]] are converted into the product.&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Primordial_soup&amp;diff=23672</id>
		<title>Primordial soup</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Primordial_soup&amp;diff=23672"/>
		<updated>2018-12-10T20:03:22Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: Cleaned up the text.&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;The Primordial soup theory was first developed by Alexander Oparin in 1942 and theorises that [[Abiogenesis|abiogenesis]] did occur in a warm water body in primordial earth. He stated that the conditions present in this primordial earth could&#039;ve given rise to early life forms, but that the earth&#039;s atmosphere had changed so radically that it was impossible to conduct experiments. &lt;br /&gt;
&lt;br /&gt;
Around the same time, J.B.S Haldane introduced his theory, which likened the primordial ocean to a chemical laboratory, containing [[organic|organic]] and [[Inorganic molecules|inorganic molecules]]. As both these theories occurred at the same time, with similarity in conclusion, the Primordial soup theory can also be named the Oparin-Haldane hypothesis&amp;lt;ref&amp;gt;Biology Wise, Finding The Origin of Life: The Primordial Soup Theory Explained.[Cited 10/12/2018] Available from: https://biologywise.com/primordial-soup-theory-explained &amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
This hypothesis gained momentum when the [[Miller-Urey experiment|Miller-Urey experiment]] managed to synthesize [[Amino-acids|amino acids]] from a chemical mixture, by simulating weather conditions that would occur in early primordial earth. However, this experiment is now scrutinised for having an [[Methane|methane]] and [[Ammonia|ammonia]] rich atmosphere which is now thought to not have been present in primordial earth. The current understanding of the primordial earth&#039;s atmosphere is now thought to be more inert, with it being [[Carbon|carbon]] and [[Nitrogen|nitrogen]] rich. In recent times, new research has shown that this atmosphere would still produce many amino acids, as the primordial soup would contain [[Iron|iron]] and carbonate materials, which neutralise [[Nitrates|nitrates]] (molecules that destroy amino acids) and [[Acidity|acidity]] (in which amino acids do not form)&amp;lt;ref&amp;gt;Fox D. Primordial Soup&#039;s On: Scientists Repeat Evolution&#039;s Most Famous Experiment. Scientific American. 2007 March. [Cited 10/12/2018} Available from: https://www.scientificamerican.com/article/primordial-soup-urey-miller-evolution-experiment-repeated/&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
=== References ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Yeast&amp;diff=23671</id>
		<title>Yeast</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Yeast&amp;diff=23671"/>
		<updated>2018-12-10T20:01:44Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: Cleaned up the text.&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;Yeast is a [[Eukaryotes|eukaryotic]], unicellular [[Organism|organism]] and belongs to the kingdom of [[Fungi|fungi]]. They can be spherical, cylindrical and filamentous. They usually replicate via [[Budding|budding]]. Budding is when a new cell grows out from the old cell and then separates from each other. Yeasts survive best in conditions with high sugar concentrations, and are able to survive both [[Anaerobic respiration|anaerobically]] and [[Aerobic respiration|aerobically]], meaning that they are [[Faculative aerobes|faculative aerobes]]&amp;lt;ref&amp;gt;Brock Biology of Microorganisms, Madigan at al, 11ed. Pearson Education, 1970, San Francisco&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
=== Types  ===&lt;br /&gt;
&lt;br /&gt;
==== &#039;&#039;Saccharomyces cerevisae&#039;&#039;  ====&lt;br /&gt;
&lt;br /&gt;
[[Saccharomyces cerevisiae|&#039;&#039;Saccharomyces cerevisiae&#039;&#039;]] (or Baker&#039;s yeast) is a common form of yeast often used as a [[Model organism|model organism]] due to its [[Eukaryotic|eukaryotic]] processes, similar to those of animal [[Cell|cells]]&amp;lt;ref&amp;gt;Alberts et al. (2008:33-34), Molecular Biology of the Cell, 5th edition, New York: Garland Science&amp;lt;/ref&amp;gt;. The presence of mitochondria in &#039;&#039;S. cerevisae&#039;&#039; is key in this. This species of yeast contains 16 chromosomes and a genome sequence that is 12.2 mb long. In addition, much has been learned about the eukaryotic cell division cycle from the study of this organism, as the yeast can reproduce sexually as well as asexually. &lt;br /&gt;
&lt;br /&gt;
This species of yeast replicates asexually by budding. [[Parent cell|Parent cells]] in cerevisiae can be differentiated by [[Scars|scars]] formed from budding, unlike in fission yeast where the daughter cells of budding yeast are smaller than the mother cell. &lt;br /&gt;
&lt;br /&gt;
==== &#039;&#039;Schizosaccharomyces pombe&#039;&#039;  ====&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;[[Schizosaccharomyces pombe|Schizosaccharomyces pombe]]&#039;&#039; (fission yeast) replicates by elongation then splitting and contains a genome sequence that is 12.5 Mb long (around 5123 genes) on 3 chromosomes. The species has an approximate homology with human disease genes of 6-7%. &#039;&#039;S. pombe&#039;&#039; is used in the production of African beer. Breakthroughs in science involve using this [[Model organism|model organism]] to study the checkpoint chemicals used to control the [[Cell cycle|cell cycle]] which is a major discovery in cancer chemistry. &lt;br /&gt;
&lt;br /&gt;
In addition, sexual reproduction may occur, in which two haploids &#039;&#039;S. cerevisiae&#039;&#039; fuse to form a [[Haploid|haploid]] cell. &lt;br /&gt;
&lt;br /&gt;
Another species; &#039;&#039;[[Candidia albicans|Candidia albicans]]&#039;&#039;, responsible for some [[Vagina|vaginial]], [[Lung|lung]] and mouth [[Infection|infections]], is a filamentous yeast. Its shape is what allows it to be [[Pathogen|pathogenic]]&amp;lt;ref&amp;gt;B Alberts, A Johnson, J Lewis, M Raff, K Roberts, P Walter, 2008, Molecular biology of the cell, 5th edition, New York: Garland Science pp. 33-34&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
=== Use in Genetic Research  ===&lt;br /&gt;
&lt;br /&gt;
Both &#039;&#039;S. cerevisiae&#039;&#039; and &#039;&#039;S. pombe&#039;&#039; are commonly used as a model organism for genetic research - particularly when looking into the cellular and genetic basis of human disease. As always with the use of model organisms in research, there are a number of advantages and disadvantages that should be considered: &lt;br /&gt;
&lt;br /&gt;
==== Advantages  ====&lt;br /&gt;
&lt;br /&gt;
*[[Unicellular|Unicellular and]] able to be grown in a defined medium &lt;br /&gt;
*Fundamental processes are conserved in all [[Eukaryotes|Eukaryotes]] &lt;br /&gt;
*Easy to manipulate [[Genome|genome]] or knockout genes &lt;br /&gt;
*Has a stable [[Haploid|haploid]]/[[Diploid|diploid]] life cycle allowing [[Complementation analysis|complementation analysis]] to identify whether mutations are present in the same or different [[Genes|genes]] &lt;br /&gt;
*Complete [[Genome|genome sequence]] is available and genes identified. This can be merged with other information from other species and played a key role in lowering the cost of genome sequencing&lt;br /&gt;
&lt;br /&gt;
==== Disadvantages  ====&lt;br /&gt;
&lt;br /&gt;
*Similar proteins may have organism-specific functions so may not function in the same way in other [[Organism|organisms of]] a different [[Species|species]] &lt;br /&gt;
*Yeast [[Genome|genome]] contains many fewer genes than the [[Human genome|human genome]] (around 6000 in yeast compared to around 30,000 in humans) &lt;br /&gt;
*Some processes in yeast are not found in other [[Eukaryotes|Eukaryotes]] &lt;br /&gt;
*Cells of different organisms live in different environments&lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Lupus&amp;diff=23670</id>
		<title>Lupus</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Lupus&amp;diff=23670"/>
		<updated>2018-12-10T19:56:55Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: Cleaned up the text. Cleaned up the references.&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;Lupus (meaning &amp;quot;wolf&amp;quot; in Latin-describing the symptom of the facial rush resembling a wolf&#039;s mask or bite) is a [[Chronic|chronic]] autoimmune disease that has no known aetiology or effective cure yet and it can be life-threatening.&amp;amp;nbsp; &lt;br /&gt;
&lt;br /&gt;
In Lupus, a larger, than usual, number of [[Antibodies|antibodies]] is produced by the immune system that attacks the healthy tissue and organs of the patient instead of protecting them from infections. This results in tissue damage and [[Inflammation|inflammation in]] almost any part of the body. &lt;br /&gt;
&lt;br /&gt;
It is considered as the greatest mimic disease since the symptoms can be non-specific and result in misdiagnoses while it resembles&amp;amp;nbsp;[[Rheumatoid arthritis|rheumatoid arthritis]] or [[Multiple Sclerosis|multiple sclerosis]]&amp;lt;ref&amp;gt;This is a reference to the official site of NHS about Lupus Disease.&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;This is a reference to the Primary Care Dermatology Society official site about Lupus.&amp;lt;/ref&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
=== Symptoms  ===&lt;br /&gt;
&lt;br /&gt;
*Symptoms of Lupus include: &lt;br /&gt;
*Headaches. &lt;br /&gt;
*Fever. &lt;br /&gt;
*Fatigue, confusion or memory loss. &lt;br /&gt;
*Chest pain. &lt;br /&gt;
*Shortness of breath. &lt;br /&gt;
*Dry eyes. &lt;br /&gt;
*Joint pain, swelling or stiffness. &lt;br /&gt;
*Butterfly face rash. &lt;br /&gt;
*[[Photosensitivity|Photosensitivity]]. &lt;br /&gt;
*[[Raynaud&#039;s phenomenon|Raynaud&#039;s phenomenon]].&amp;amp;nbsp;&lt;br /&gt;
&lt;br /&gt;
=== Types of Lupus:  ===&lt;br /&gt;
&lt;br /&gt;
There are four types of Lupus: &lt;br /&gt;
&lt;br /&gt;
==== 1. Systemic Lupus Erythematosus:  ====&lt;br /&gt;
&lt;br /&gt;
The most common type of Lupus that can be mild or severe. It contains inflammation of the kidneys, nervous system, brain&#039;s blood vessels and hardening of arteries. &lt;br /&gt;
&lt;br /&gt;
==== 2. Cutaneous Lupus Erythematosus:  ====&lt;br /&gt;
&lt;br /&gt;
This type of Lupus is limited to the skin causing many types of rashes and sores, mostly on the face area. &lt;br /&gt;
&lt;br /&gt;
==== 3. Drug-induced Lupus Erythematosus:  ====&lt;br /&gt;
&lt;br /&gt;
Lupus disease caused by certain drug prescription such as Hydralazine (high blood pressure/hypertension), Procainamide (irregular heart rhythms) and Isoniazid (tuberculosis). &lt;br /&gt;
&lt;br /&gt;
==== 4. Neonatal Lupus:  ====&lt;br /&gt;
&lt;br /&gt;
Not an actual type of Lupus. It is caused by a mother having Lupus having her antibodies to the infant in the womb&amp;lt;ref&amp;gt;This is a reference for the Mayo Clinic official site about Lupus.&amp;lt;/ref&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Lupus&amp;diff=23669</id>
		<title>Lupus</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Lupus&amp;diff=23669"/>
		<updated>2018-12-10T19:53:27Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;Lupus (meaning &amp;quot;wolf&amp;quot; in Latin-describing the symptom of the facial rush resembling a wolf&#039;s mask or bite) is a [[Chronic|chronic]] autoimmune disease that has no known aetiology or effective cure yet and it can be life-threatening.&amp;amp;nbsp; &lt;br /&gt;
&lt;br /&gt;
In Lupus, a larger, than usual, number of [[Antibodies|antibodies]] is produced by the immune system that attack the healthy tissue and organs of the patient instead of protecting them from infections. This results in tissue damage and [[Inflammation|inflammation in]] almost any part of the body. &lt;br /&gt;
&lt;br /&gt;
It is considered as the greatest mimic disease since the symptoms can be non-specific and result in misdiagnoses while it resembles&amp;amp;nbsp;[[Rheumatoid arthritis|rheumatoid arthritis]] or [[Multiple Sclerosis|multiple sclerosis]]&amp;lt;ref&amp;gt;This is a reference to the official site of NHS about Lupus Disease.&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;This is a reference to the Primary Care Dermatology Society official site about Lupus.&amp;lt;/ref&amp;gt;.&amp;lt;br&amp;gt; &lt;br /&gt;
&lt;br /&gt;
=== Symptoms&amp;lt;br&amp;gt;  ===&lt;br /&gt;
&lt;br /&gt;
*Symptoms of Lupus include: &lt;br /&gt;
*Headaches. &lt;br /&gt;
*Fever. &lt;br /&gt;
*Fatigue, confusion or memory loss. &lt;br /&gt;
*Chest pain. &lt;br /&gt;
*Shortness of breath. &lt;br /&gt;
*Dry eyes. &lt;br /&gt;
*Joint pain, swelling or stiffness. &lt;br /&gt;
*Butterfly face rash. &lt;br /&gt;
*[[Photosensitivity|Photosensitivity]]. &lt;br /&gt;
*[[Raynaud&#039;s phenomenon|Raynaud&#039;s phenomenon]].&amp;amp;nbsp;&lt;br /&gt;
&lt;br /&gt;
=== Types of Lupus&amp;lt;br&amp;gt;  ===&lt;br /&gt;
&lt;br /&gt;
There are four types of Lupus:&lt;br /&gt;
&lt;br /&gt;
==== 1. Systemic Lupus Erythematosus:  ====&lt;br /&gt;
&lt;br /&gt;
The most common type of Lupus that can be mild or severe. It contains inflammation of the kidneys, nervous system, brain&#039;s blood vessels and hardening of arteries. &lt;br /&gt;
&lt;br /&gt;
====   ====&lt;br /&gt;
&lt;br /&gt;
This type of Lupus is limited to the skin causing many types of rashes and sores, mostly on the face area. &lt;br /&gt;
&lt;br /&gt;
====   ====&lt;br /&gt;
&lt;br /&gt;
Lupus disease caused by certain drug prescription such as Hydralazine (high blood pressure/hypertension), Procainamide (irregular heart rhythms) and Isoniazid (tuberculosis). &lt;br /&gt;
&lt;br /&gt;
==== 4. Neonatal Lupus:  ====&lt;br /&gt;
&lt;br /&gt;
Not an actual type of Lupus. It is caused by a mother having Lupus having her antibodies to the infant in the womb&amp;lt;ref&amp;gt;This is a reference for the Mayo Clinic official site about Lupus.&amp;lt;/ref&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;&amp;lt;references /&amp;gt;&#039;&#039;&#039; &lt;br /&gt;
&lt;br /&gt;
&amp;amp;nbsp; &amp;amp;nbsp; &amp;amp;nbsp; &amp;amp;nbsp; &amp;amp;nbsp; &amp;amp;nbsp; &amp;amp;nbsp; &amp;amp;nbsp; &amp;amp;nbsp; &amp;amp;nbsp; &amp;amp;nbsp; &amp;amp;nbsp; &amp;amp;nbsp; &amp;amp;nbsp; &amp;amp;nbsp;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Exothermic_reaction&amp;diff=23668</id>
		<title>Exothermic reaction</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Exothermic_reaction&amp;diff=23668"/>
		<updated>2018-12-10T19:51:00Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;An exothermic reaction is a chemical reaction in which the heat energy of the surroundings increases, due to the release of energy from [[Bond|chemical bonds]]. The opposite of an exothermic reaction is an [[Endothermic reaction|endothermic reaction]] in which the heat energy is taken in as opposed to given out. An exothermic reaction can be called a &#039;heat giving&#039; reaction. Exothermic reactions are associated with the making of stronger chemical bonds. &lt;br /&gt;
&lt;br /&gt;
=== &#039;&#039;&#039;Examples of Exothermic Reactions:&#039;&#039;&#039;  ===&lt;br /&gt;
&lt;br /&gt;
*Combustion reactions of fuels or a substance &lt;br /&gt;
*[[Neutralization|Neutralization]] &lt;br /&gt;
*Deposition of dry ice ([[carbon dioxide|carbon dioxide]]) from the gaseous state &lt;br /&gt;
*Adding water to [[anhydrous copper(II) sulphate|anhydrous copper(II) sulphate]]&lt;br /&gt;
*[http://www.davidavery.co.uk/thermite/ The thermite reaction] &lt;br /&gt;
*Reactions taking place in a self-heating can be based on lime aluminium &lt;br /&gt;
*Many corrosion reactions such as [[Oxidation|oxidation]] of metals &lt;br /&gt;
*Decomposition of vegetable matter into compost &lt;br /&gt;
*Solution of [[sulphuric acid|sulphuric acid]] into [[water|water]]&lt;br /&gt;
*[[Dehydration|Dehydration]] of sugars upon contact with sulfuric acid &lt;br /&gt;
*Detonation of nitroglycerin &lt;br /&gt;
*Nuclear fission of uranium-235&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Patau%27s_Syndrome&amp;diff=23667</id>
		<title>Patau&#039;s Syndrome</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Patau%27s_Syndrome&amp;diff=23667"/>
		<updated>2018-12-10T19:49:56Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: Refs not added correctly. Cleaned up the references. No links. Added some links.&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;Patau&#039;s syndrome is actually by a [[chromatic aneuploidy|chromatic aneuploidy]], which means the addition of an extra [[chromosome|chromosome]]. This is referred to as an abnormality, which is often responsible for genetic diseases within clinical genetics. Patau&#039;s syndrome specifically is caused by [[trisomy 13|trisomy 13]], in which there is a third [[chromosome 13|chromosome 13]]. This is called an [[unbalanced Robertsonian translocation|unbalanced Robertsonian translocation]]; unbalanced due to the chromosome abnormality, and a translocation because this chromosome is not actually at the 13 chromosome position in a [[karyotype|karyotype]] but in the [[chromosome 14|chromosome 14]] position. &lt;br /&gt;
&lt;br /&gt;
Patau&#039;s syndrome is a disease correlating with severe intellectual disability and physical abnormalities&amp;lt;ref&amp;gt;US National Library of Medicine 2018 [cited 4/12/2018] Available from: https://ghr.nlm.nih.gov/condition/trisomy-13&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;US National Library of Medicine 2017 [cited 31/1/2017] Available from: www.nichd.nih.gov/health/topics/down/conditioninfo/symptoms&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Semi-permeable_membrane&amp;diff=23666</id>
		<title>Semi-permeable membrane</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Semi-permeable_membrane&amp;diff=23666"/>
		<updated>2018-12-10T19:47:11Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;A Semi-permeable membrane is one of the different types of biological or artificial membranes which only allows certain [[molecules|molecules]] or [[ions|ions]] to pass through it. Artificial membranes such as those used in [[Reverse osmosis|reverse osmosis]], are designed with a variety of materials for the purpose of filtration and they only allow water to pass through&amp;lt;ref&amp;gt;https://biologydictionary.net/semipermeable-membrane/&amp;lt;/ref&amp;gt;. The Biological membranes of the cells however are found in a [[Phospholipid bilayer|phospholipid bilayer]] form. [[Water|Water]] and other such smaller [[molecules|molecules]] pass through the gaps in the bilayer but larger molecules or ions cannot force their way in or out of the [[cell|cell]].&amp;lt;br&amp;gt; &lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=ATPase_Pumps&amp;diff=23665</id>
		<title>ATPase Pumps</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=ATPase_Pumps&amp;diff=23665"/>
		<updated>2018-12-10T19:46:23Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: Cleaned up the references.&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;Within [[Active transport]] there are three different types of ubiquitous ATPase pumps found in all cell types. Their main function is to pump small molecules across small membranes, achieved through the [[Hydrolysis]] of [[ATP]] to [[ADP|ADP]] and Pi which releases energy driving the passage of [[Molecules|molecules]] across the membrane. The three types of pump are: &lt;br /&gt;
&lt;br /&gt;
#[[P-type pumps]]: P-type pumps are transmembrane proteins and are so called as they [[Phosphorylation|phosphorylate]] themselves during the pump cycle. They are laregly responsible for maintaining the concentration gradient of ions such as Na&amp;lt;sup&amp;gt;+&amp;lt;/sup&amp;gt; and K&amp;lt;sup&amp;gt;+ &amp;lt;/sup&amp;gt;across [[Cell membranes|cell membranes]]. &lt;br /&gt;
#[[F-type pumps|F-type pumps]]: These pumps are turbine shaped and are made up of many different subunits. They differ structurally from [[P-type pumps]] and are found in the plasma membrane of bacteria and the inner membrane of [[Mitochondria]]. They work in reverse compared to the other pumps as the H&amp;lt;sup&amp;gt;+&amp;lt;/sup&amp;gt; gradient is used to drive the synthesis of ATP from ADP and Pi and so are referred to as [[ATP synthase|ATP synthases]]. V-Type ATPases, for example, use the energy from the hydrolysis of ATP to set up a concentration gradient of H+ through a proton pump. This movement of H+ ions allows for acidification that is essential in many biological processes. In the kidney for example, V-type ATPases in the late distal convoluted tubule power the active transport of H+ into the urine across epithelial cells. This results in the urine remaining sufficiently acidic and in turn, prevents subsequent disorders, such as renal tubule acidosis, from occurring&amp;lt;ref&amp;gt;NCBI. Regulation and Isoform function of the V-ATPases. 2015 [cited 18/11/18]; Available from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2907102/&amp;lt;/ref&amp;gt;. &lt;br /&gt;
#[[ABC transporters|ABC transporters]]: ABC transporters differ as unlike the other pumps which only selectively pump ions, they also pump other small uncharged moleules&amp;lt;ref&amp;gt;Alberts, A., Johnson, A., Lewis, J., Raff, M., Roberts, K., and Walter, P. (2008) Molecular Biology of the Cell, fifth edition, New York: Garland Science.&amp;lt;/ref&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Methylation&amp;diff=23664</id>
		<title>Methylation</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Methylation&amp;diff=23664"/>
		<updated>2018-12-10T19:44:55Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;Methylation is a form of [[Alkylation|alkylation]], i.e. the transfer of an [[Alkyl group|alkyl group]] to another [[Molecule|molecule]]. Methylation is specifically the addition or substition of a [[Methyl|methyl group]] to a molecule. [[Methyl groups|Methyl groups]] are alkyls made from [[Methane|methane]] and are [[Carbon|carbon]] [[Atoms|atoms]] attached to 3 [[Hydrogen|hydrogen]] atoms -CH&amp;lt;sub&amp;gt;3&amp;lt;/sub&amp;gt;&amp;lt;ref&amp;gt;March&#039;s Advanced Organic Chemistry. Michael B. Smith, Jerry March - John Wiley and Sons (2007)&amp;lt;/ref&amp;gt;. It can be involved in the [[Gene expression|expression of genes]], as well as [[Protein|protein]] function regulation and the metabolism of [[RNA|RNA]]. An example of this is the tri-methylation of [[Lysine|lysine]] 36 on the H3 protein (of a histone), which is involved in the response of plants to necrotrophic fungal attack&amp;lt;ref&amp;gt;http://www.plantphysiol.org/content/154/3/1403&amp;lt;/ref&amp;gt;.&amp;amp;nbsp; &lt;br /&gt;
&lt;br /&gt;
Methylation of a [[gene|gene]], addition of a [[methyl group|methyl group]] (-CH&amp;lt;sub&amp;gt;3&amp;lt;/sub&amp;gt;), is catalyzed by the family of enzymes [[DNA-methyltransferases|DNA-methyltransferases]] (DNMTs) and occurs at the 5-carbon on a cytosine ring; the methyl group projects into the major groove of the DNA double helix, causing the DNA-histone complex to become more tightly condensed, which prevents/negatively affects the binding of transcriptional factors to promoter regions or induces deacetylation of the histone proteins which inhibits transcription of the DNA sequence to mRNA. &lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Evolution&amp;diff=23663</id>
		<title>Evolution</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Evolution&amp;diff=23663"/>
		<updated>2018-12-10T19:44:06Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: Cleaned up the references. Cleaned up the text.&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;&amp;quot;Nothing in biology makes sense except in the light of evolution.&amp;quot;&#039;&#039; - [http://en.wikipedia.org/wiki/Nothing_in_Biology_Makes_Sense_Except_in_the_Light_of_Evolution Theodosius Dobzhansky]. &lt;br /&gt;
&lt;br /&gt;
The word evolution has been defined as &amp;quot;the gradual developing of something&amp;quot;&amp;lt;ref&amp;gt;http://oxforddictionaries.com/definition/evolution&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
Some argue that evolution is strictly the change over time, in [[Genes|genes]] and [[Proteins|proteins]], that occur in a population which allow an organism to be advantageous in its surrounding environment. Organisms change continuously over time due to random mutations; however, the aforementioned definition incorporates that these changes - the evolution of a certain organism, must be beneficial in terms of its environment. &lt;br /&gt;
&lt;br /&gt;
Evolutionary changes in metabolism, development and behaviour created three domains&amp;lt;ref&amp;gt;Hartl, D.L. and Ruvolo, M. (2011) &#039;Genetics: Analysis of Genes and Genomes.&#039; 8th edn. Burlington: Jones and Bartlett Learning.&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;University of California Museum of Paleontology. (). Mechanisms of Change. Available: http://www.evolution.berkeley.edu.&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;Bruce Alberts, Alexander Johnson, Julian Lewis, Martin Raff, Keith Roberts, Peter Walter. (2008) Molecular Biology of the Cell, 5th edition, New York: Garland Science&amp;lt;/ref&amp;gt;: &lt;br /&gt;
&lt;br /&gt;
*[[Bacteria|Bacteria]] &lt;br /&gt;
*[[Archaea|Archaea]] &lt;br /&gt;
*[[Eukarya|Eukarya]]&lt;br /&gt;
&lt;br /&gt;
Causes of evolution are mutation, migration, genetic drift and natural selection. &lt;br /&gt;
&lt;br /&gt;
The first scientist in history that explained how evolution works and hypothesized the theory of natural selection was Charles Darwin. &lt;br /&gt;
&lt;br /&gt;
[[Charles Darwin|Charles Darwin]] proposed the theory of [[Natural selction|natural selction]] which entails that it is the key mechanism of evolution as it is based on the change of heritable traits of a population over generations. Due to mutations and adaptions, some individuals develop characteristics that are selected for the environment and it helps them survive, whereas other individuals develop characteristics that are selected against the environment and it puts them in disadvantage. Therefore, the individuals that are selected for and are well adapted will reproduce within themselves and the poorly adapted organisms will not pass on their traits to an offspring. This results in a big sample of well-adapted population with traits that are better selected for survival over generations whereas there will be fewer and fewer individuals that are poorly adapted over a generation. From this situation, the term &amp;quot;survival of the fittest&amp;quot; was created where the strongest individuals are bound to survive and pass on their traits within a harsh environment&amp;lt;ref&amp;gt;What Is Evolution?&amp;quot;. 2018. BBC Bitesize. Accessed December 10 2018. https://www.bbc.com/bitesize/articles/z9qs4qt.&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Deoxynucleotide&amp;diff=23662</id>
		<title>Deoxynucleotide</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Deoxynucleotide&amp;diff=23662"/>
		<updated>2018-12-10T19:41:23Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: Added the references correctly. Cleaned up the text. Added some links.&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;A deoxynucleotide in biological terms is a component of [[Deoxyribonucleic_acid|deoxyribonucleic acid]], [[DNA|DNA]]. A deoxynucleotide is made up of an organic base, a [[Ribose|ribose sugar]] and [[phosphate|phosphate]]. [[DNA polymerase|DNA polymerase]] requires deoxynucleotides in their triphosphate (containing three phosphates) form in order for [[DNA synthesis|DNA synthesis]] to take place&amp;lt;ref&amp;gt;groups.molbiosci.northwestern.edu/holmgren/Glossary/Definitions/Def-D/deoxynucleotide.html&amp;lt;/ref&amp;gt;. The 4 triphosphates ([[DNTP|dNTPs]]) are [[ATP|ATP]], [[CTP|CTP]], [[GTP|GTP]] and [[TTP|TTP]], one for each organise base – [[adenine|adenine]], [[cytosine|cytosine]], [[guanine|guanine]] and [[thymine|thymine]] relatively. &lt;br /&gt;
&lt;br /&gt;
Deoxynucleotide triphosphates are an essential component of nucleic acid [[molecules|molecules]] and are required in [[PCR|PCR]] (polymerase chain reaction), a technique used in genetics that analyses a short sequence of DNA and used to amplify sections of DNA that are wanted and required&amp;lt;ref&amp;gt;www.medicinenet.com/script/main/art.asp&amp;lt;/ref&amp;gt;. No amplified DNA would be able to be made without dNTPs&amp;lt;ref&amp;gt;ink.springer.com/chapter/10.1007/978-1-4020-6241-4_6&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Streptococcus_pneumoniae&amp;diff=23661</id>
		<title>Streptococcus pneumoniae</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Streptococcus_pneumoniae&amp;diff=23661"/>
		<updated>2018-12-10T19:37:19Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;Streptococcus pneumoniae&#039;&#039; is an infectious bacterium which causes many diseases incuding [[Pneumonia|pneumonia]]&amp;lt;ref&amp;gt;Centres for Disease Control and Prevention. Traveler&#039;s Health: Pneumococcal Disease - Streptococcus pneumoniae. 2014. Available at: https://wwwnc.cdc.gov/travel/diseases/pneumococcal-disease-streptococcus-pneumoniae. [Accessed on: 05/12/17]&amp;lt;/ref&amp;gt;. &#039;&#039;S. pneumoniae &#039;&#039;is a [[Gram-positive|Gram-positive]] bacteria&amp;lt;ref&amp;gt;Centre for Disease Control and Prevention. Pneumococcal Disease - Streptococcus pneumoniae. 2017. Available at: https://www.cdc.gov/pneumococcal/clinicians/streptococcus-pneumoniae.html [Accessed on: 05/12/2017]&amp;lt;/ref&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
&#039;&#039;S. pneumoniae&#039;&#039; is part of the genus Strepotococcus&amp;lt;ref&amp;gt;http://perspectivesinmedicine.cshlp.org/content/3/7/a010215.full&amp;lt;/ref&amp;gt;. . They are usually found in pairs ([[Diplococci|diplococci]]) and are an example of a highly invasive pathogen. It is the main cause of pneumonia and meningitis in children and in the elderly. There are 2 types of &#039;&#039;S. pneumoniae &#039;&#039;infection; invasive (Infections of organs and blood, which are typically more harmful) and non-invasive (infections outside of major organs and blood, which are typically less harmful). Treatment for the different types of infection vary, with invasive strains being treated with antibiotics (either administered at home or hospital) and non-invasive strains usually go away without any need for serious treatment. Those at a higher risk of developing a &#039;&#039;S. pneumoniae&#039;&#039; infection are those with weakened immune systems (either due to illnesses, such as HIV, or those on medication that weakens the immune system, young children and elderly people). 2 types of vaccination can be given to reduce the chance of infection, these can either be pneumococcal conjugate vaccine (PCV) which is given to young children, or pneumococcal polysaccharide vaccine (PPV) which is typically given to elderly people and those at high risk of infection. &lt;br /&gt;
&lt;br /&gt;
&#039;&#039;S. pneumoniae&#039;&#039; normally live as part of the natural bacterial flora that exists in the upper respiratory tract, however, unusually high amounts of the bacteria causes it to disrupt the balance of the system, allowing it to move and spread into the lungs, sinuses, and ears&amp;lt;ref&amp;gt;Aljecivic M, Karcic E, Bektas S, Karcic B, Representation of Streptococcus Pneumoniae in Outpatient Population of Sarajevo Canton, Medical Archives, 2015, 69(3), 177-180, Available from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4500380/.&amp;lt;/ref&amp;gt;. This can lead to an infection of the microbe, potentially causing pneumonia. &lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Pi&amp;diff=23660</id>
		<title>Pi</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Pi&amp;diff=23660"/>
		<updated>2018-12-10T19:35:56Z</updated>

		<summary type="html">&lt;p&gt;Nnjm2: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;Pi (not to be confused with the number Pi) in the biological sciences is most commonly known as &#039;&#039;&#039;inorganic phosphate&#039;&#039;&#039;. It is a free [[Ions|ion]] in solution and the term Pi is used to distinguish it from phosphates found in phosphate esters. At physiological pH (6.8 - 7.0), inorganic phosphate consists of largely HPO&amp;lt;sub&amp;gt;4&amp;lt;/sub&amp;gt;&amp;lt;sup&amp;gt;2-&amp;lt;/sup&amp;gt; and H&amp;lt;sub&amp;gt;2&amp;lt;/sub&amp;gt;PO&amp;lt;sub&amp;gt;4&amp;lt;/sub&amp;gt;&amp;lt;sup&amp;gt;2-&amp;lt;ref&amp;gt;Stryer et al. Biochemistry 7th Edition. 2011. Page 16&amp;lt;/ref&amp;gt;.&amp;lt;/sup&amp;gt; &lt;br /&gt;
&lt;br /&gt;
However, phosphates are most commonly found in the form of adenosine phosphates, ([[AMP|AMP]], [[ADP|ADP]] and [[ATP|ATP]]) and in [[DNA|DNA]] and RNA and Pi is released by the hydrolysis of [[ATP|ATP]] or [[ADP|ADP]], if [[ATP|ATP]] is hydrolysed to [[AMP|AMP]], [[Pyrophosphate|pyrophosphate]] (PPi) is formed. The addition and removal of phosphate as seen through [[Phosphorylation|phosphorylation]] and [[Dephosphorylation|dephosphorylation]] is crucial for many metabolic pathways. &lt;br /&gt;
&lt;br /&gt;
=== References  ===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;references /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Nnjm2</name></author>
	</entry>
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