Protein secondary stucture - Revision history

Nnjm2: Cleaned up the text. Cleaned up the references.

2018-11-19T19:05:14Z

Cleaned up the text. Cleaned up the references.

← Older revision		Revision as of 19:05, 19 November 2018
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	The secondary structure of a protein describes the way in which a polypeptide chain of [[~~Amino_acids~~\|amino acids]] are folded.~~<br>~~These secondary structures can be separated into 2 section [[Alpha-helix\|alpha-helicies]] and a [[Beta-sheet\|beta-sheet]] formation, these describe the level of organisation of the specific ~~foldin patterens~~.		The secondary structure of a protein describes the way in which a polypeptide chain of [[Amino acids\|amino acids]] are folded. These secondary structures can be separated into 2 section [[Alpha-helix\|alpha-helicies]] and a [[Beta-sheet\|beta-sheet]] formation, these describe the level of organisation of the specific folding patterns.

	=== Alpha-Helix ===		=== Alpha-Helix ===

	A alpha-helix is a right handed helix that resembles a right handed spiral staircase. An alpha helix contains [[~~Hydrogen_Bonding~~\|hydrogen bonding]] between the~~ ~~N-H group~~ ~~of every peptide bond and C=O groups that~~ ~~are next to a peptide bond<ref>B.Alberts et al. (2014) Essencial Cell Biology 4th edition, Gartland Science, New York</ref>. these are usually ~~loacated~~ 4 [[Amino acid\|amino acids]] away~~ ~~from each other but in the same chain. This is what produces the ~~spiraling~~ structure of the alpha-helix. There is 3.6 amino acid residues in each coil turn in the alpha helix.<ref>Berg.J, Stryer.L, Tymoczko J, Biochemistry, seventh edition, WH Freeman, 2012, page 39</ref>~~ ~~		An alpha-helix is a right-handed helix that resembles a right-handed spiral staircase. An alpha helix contains [[Hydrogen Bonding\|hydrogen bonding]] between the N-H group of every peptide bond and C=O groups that are next to a peptide bond<ref>B. Alberts et al. (2014) Essencial Cell Biology 4th edition, Gartland Science, New York</ref>. these are usually located 4 [[Amino acid\|amino acids]] away from each other but in the same chain. This is what produces the spiralling structure of the alpha-helix. There is 3.6 amino acid residues in each coil turn in the alpha helix<ref>Berg.J, Stryer.L, Tymoczko J, Biochemistry, seventh edition, WH Freeman, 2012, page 39</ref>.

	The most common known helix structure is that of [[DNA\|DNA]], where 2 alpha ~~helicies~~ are wound around each other with ~~complimentary~~ base ~~paring~~ between them holding them together.		The most common known helix structure is that of [[DNA\|DNA]], where 2 alpha helices are wound around each other with the complementary base pairing between them holding them together.

	=== Beta-Sheet ===		=== Beta-Sheet ===

	The beta-sheet is where one chain of amino acids, form a parallel or~~ ~~antiparallel folded structure with [[Hydrogen bond\|hydrogen bonding]] between the ~~ajacent~~ strands~~ ~~of the fold, between N-H and C=O~~ ~~groups.<ref>B.Alberts et al. (2014) ~~Essencial~~ Cell Biology 4th edition, Gartland Science, New York</ref>		The beta-sheet is where one chain of amino acids, form a parallel or antiparallel folded structure with [[Hydrogen bond\|hydrogen bonding]] between the adjacent strands of the fold, between N-H and C=O groups<ref>B. Alberts et al. (2014) Essential Cell Biology 4th edition, Gartland Science, New York</ref>.

	The antiparallel structure is stronger due to the almost perfect lining up of the strands to make hydrogen bonds that form directly ~~perpendiculatr~~ to the running strand. The parallel structure isn't as strong however it is still a very ~~ridged~~ structure. Sometimes, these beta sheets are able to twist, thus they are able to form a barrel shape. This is useful tool as this means they form ~~cylindral~~ structures which can, for example, be used as passageways and pores~~. ~~<ref>Petsko.G, Ringe.D, Protein Structure and Function, New Science Press, 2004, page 16</ref>		The antiparallel structure is stronger due to the almost perfect lining up of the strands to make hydrogen bonds that form directly perpendicular to the running strand. The parallel structure isn't as strong however it is still a very rigid structure. Sometimes, these beta sheets are able to twist, thus they are able to form a barrel shape. This is a useful tool as this means they form cylindrical structures which can, for example, be used as passageways and pores<ref>Petsko.G, Ringe.D, Protein Structure and Function, New Science Press, 2004, page 16</ref>.

	=== References ===		=== References ===

	<references />		<references />

180236899: added a couple links and corrected some grammar.

2018-11-19T17:26:10Z

added a couple links and corrected some grammar.

← Older revision		Revision as of 17:26, 19 November 2018
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	The secondary structure of a protein describes the way in which a ~~poly peptide~~ chain of amino acids are folded.<br>These secondary structures can be separated into 2 section [[Alpha-helix\|alpha-helicies]] and a [[Beta-sheet\|beta-sheet]] formation, these describe the level of organisation of the specific foldin patterens.		The secondary structure of a protein describes the way in which a polypeptide chain of [[Amino_acids\|amino acids]] are folded.<br>These secondary structures can be separated into 2 section [[Alpha-helix\|alpha-helicies]] and a [[Beta-sheet\|beta-sheet]] formation, these describe the level of organisation of the specific foldin patterens.

	=== Alpha-Helix ===		=== Alpha-Helix ===

	A alpha-helix is a right handed helix that resembles a right handed spiral staircase. An alpha helix contains hydrogen bonding between the N-H group of every peptide bond and C=O groups that are next to a peptide bond<ref>B.Alberts et al. (2014) Essencial Cell Biology 4th edition, Gartland Science, New York</ref>. these are usually loacated 4 [[Amino acid\|amino acids]] away from each other but in the same chain. This is what produces the spiraling structure of the alpha-helix. There is 3.6 amino acid residues in each coil turn in the alpha helix.<ref>Berg.J, Stryer.L, Tymoczko J, Biochemistry, seventh edition, WH Freeman, 2012, page 39</ref>		A alpha-helix is a right handed helix that resembles a right handed spiral staircase. An alpha helix contains [[Hydrogen_Bonding\|hydrogen bonding]] between the N-H group of every peptide bond and C=O groups that are next to a peptide bond<ref>B.Alberts et al. (2014) Essencial Cell Biology 4th edition, Gartland Science, New York</ref>. these are usually loacated 4 [[Amino acid\|amino acids]] away from each other but in the same chain. This is what produces the spiraling structure of the alpha-helix. There is 3.6 amino acid residues in each coil turn in the alpha helix.<ref>Berg.J, Stryer.L, Tymoczko J, Biochemistry, seventh edition, WH Freeman, 2012, page 39</ref>

	The most common known helix structure is that of [[DNA\|DNA]], where 2 alpha helicies are wound around each other with complimentary base paring between them holding them together.		The most common known helix structure is that of [[DNA\|DNA]], where 2 alpha helicies are wound around each other with complimentary base paring between them holding them together.

	=== Beta-Sheet ===		=== Beta-Sheet ===
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	The beta-sheet is where one chain of amino acids, form a parallel or antiparallel folded structure with [[Hydrogen bond\|hydrogen bonding]] between the ajacent strands of the fold, between N-H and C=O groups.<ref>B.Alberts et al. (2014) Essencial Cell Biology 4th edition, Gartland Science, New York</ref>		The beta-sheet is where one chain of amino acids, form a parallel or antiparallel folded structure with [[Hydrogen bond\|hydrogen bonding]] between the ajacent strands of the fold, between N-H and C=O groups.<ref>B.Alberts et al. (2014) Essencial Cell Biology 4th edition, Gartland Science, New York</ref>

	The antiparallel structure is stronger due to the almost perfect lining up of the strands to make hydrogen bonds that form directly perpendiculatr to the running strand. The parallel structure isn't as strong however it is still a very ridged structure. Sometimes, these beta sheets are able to twist, thus they are able to form a barrel shape. This is useful tool as this means they form cylindral structures which can, for example, be used as passageways and pores. <ref>Petsko.G, Ringe.D, Protein Structure and Function, New Science Press, 2004, page 16</ref>		The antiparallel structure is stronger due to the almost perfect lining up of the strands to make hydrogen bonds that form directly perpendiculatr to the running strand. The parallel structure isn't as strong however it is still a very ridged structure. Sometimes, these beta sheets are able to twist, thus they are able to form a barrel shape. This is useful tool as this means they form cylindral structures which can, for example, be used as passageways and pores. <ref>Petsko.G, Ringe.D, Protein Structure and Function, New Science Press, 2004, page 16</ref>

	=== References ===		=== References ===

	<references />		<references />

140254312 at 21:12, 27 November 2014

2014-11-27T21:12:53Z

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	=== Beta-Sheet ===		=== Beta-Sheet ===

	The beta-sheet is where one chain of amino acids, form a parallel or antiparallel folded structure with [[~~Hydrogen_bond~~\|hydrogen bonding]] between the ajacent strands of the fold, between N-H and C=O groups.<ref>B.Alberts et al. (2014) Essencial Cell Biology 4th edition, Gartland Science, New York</ref>		The beta-sheet is where one chain of amino acids, form a parallel or antiparallel folded structure with [[Hydrogen bond\|hydrogen bonding]] between the ajacent strands of the fold, between N-H and C=O groups.<ref>B.Alberts et al. (2014) Essencial Cell Biology 4th edition, Gartland Science, New York</ref>

	The antiparallel structure is stronger due to the almost perfect lining up of the strands to make hydrogen bonds that form directly perpendiculatr to the running strand. The parallel structure isn't as strong ~~howevre~~ is still a very ridged structure.		The antiparallel structure is stronger due to the almost perfect lining up of the strands to make hydrogen bonds that form directly perpendiculatr to the running strand. The parallel structure isn't as strong however it is still a very ridged structure. Sometimes, these beta sheets are able to twist, thus they are able to form a barrel shape. This is useful tool as this means they form cylindral structures which can, for example, be used as passageways and pores. <ref>Petsko.G, Ringe.D, Protein Structure and Function, New Science Press, 2004, page 16</ref>

	=== References ===		=== References ===

	<references />		<references />

140254312 at 21:07, 27 November 2014

2014-11-27T21:07:17Z

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	=== Alpha-Helix ===		=== Alpha-Helix ===

	A alpha-helix is a right handed helix that resembles a right handed spiral staircase. An alpha helix contains hydrogen bonding between the N-H group of every peptide bond and C=O groups that are next to a peptide bond<ref>B.Alberts et al. (2014) Essencial Cell Biology 4th edition, Gartland Science, New York</ref>. these are usually loacated 4 [[~~Amino_acid~~\|amino acids]] away from each other but in the same chain. This is what produces the spiraling structure of the alpha-helix.		A alpha-helix is a right handed helix that resembles a right handed spiral staircase. An alpha helix contains hydrogen bonding between the N-H group of every peptide bond and C=O groups that are next to a peptide bond<ref>B.Alberts et al. (2014) Essencial Cell Biology 4th edition, Gartland Science, New York</ref>. these are usually loacated 4 [[Amino acid\|amino acids]] away from each other but in the same chain. This is what produces the spiraling structure of the alpha-helix. There is 3.6 amino acid residues in each coil turn in the alpha helix.<ref>Berg.J, Stryer.L, Tymoczko J, Biochemistry, seventh edition, WH Freeman, 2012, page 39</ref>

	The most common known helix structure is that of [[DNA\|DNA]], where 2 alpha helicies are wound around each other with complimentary base paring between them holding them together.		The most common known helix structure is that of [[DNA\|DNA]], where 2 alpha helicies are wound around each other with complimentary base paring between them holding them together.

	=== Beta-Sheet ===		=== Beta-Sheet ===

Nnjm2 at 02:27, 29 November 2013

2013-11-29T02:27:43Z

← Older revision		Revision as of 02:27, 29 November 2013
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	The secondary structure of a protein describes the way in which a poly peptide chain of amino acids are folded.<br>These secondary structures can be separated into 2 section alpha-helicies and a beta-sheet formation, these describe the level of organisation of the specific foldin patterens.		The secondary structure of a protein describes the way in which a poly peptide chain of amino acids are folded.<br>These secondary structures can be separated into 2 section [[Alpha-helix\|alpha-helicies]] and a [[Beta-sheet\|beta-sheet]] formation, these describe the level of organisation of the specific foldin patterens.

	=== Alpha-Helix ===		=== Alpha-Helix ===

	A alpha-helix is a right handed helix that resembles a right handed spiral staircase. An alpha helix contains hydrogen bonding between the N-H group of every peptide bond and C=O groups that are next to a peptide bond<ref>B.Alberts et al. (2014) Essencial Cell Biology 4th edition, Gartland Science, New York</ref>. these are usually loacated 4 amino acids away from each other but in the same chain. This is what produces the spiraling structure of the alpha-helix.		A alpha-helix is a right handed helix that resembles a right handed spiral staircase. An alpha helix contains hydrogen bonding between the N-H group of every peptide bond and C=O groups that are next to a peptide bond<ref>B.Alberts et al. (2014) Essencial Cell Biology 4th edition, Gartland Science, New York</ref>. these are usually loacated 4 [[Amino_acid\|amino acids]] away from each other but in the same chain. This is what produces the spiraling structure of the alpha-helix.

	The most common known helix structure is that of DNA, where 2 alpha helicies are wound around each other with complimentary base paring between them holding them together.		The most common known helix structure is that of [[DNA\|DNA]], where 2 alpha helicies are wound around each other with complimentary base paring between them holding them together.

	=== Beta-Sheet ===		=== Beta-Sheet ===

	The beta-sheet is where one chain of amino acids, form a parallel or antiparallel folded structure with hydrogen bonding between the ajacent strands of the fold, between N-H and C=O groups.<ref>B.Alberts et al. (2014) Essencial Cell Biology 4th edition, Gartland Science, New York</ref>		The beta-sheet is where one chain of amino acids, form a parallel or antiparallel folded structure with [[Hydrogen_bond\|hydrogen bonding]] between the ajacent strands of the fold, between N-H and C=O groups.<ref>B.Alberts et al. (2014) Essencial Cell Biology 4th edition, Gartland Science, New York</ref>

	The antiparallel structure is stronger due to the almost perfect lining up of the strands to make hydrogen bonds that form directly perpendiculatr to the running strand. The parallel structure isn't as strong howevre is still a very ridged structure.		The antiparallel structure is stronger due to the almost perfect lining up of the strands to make hydrogen bonds that form directly perpendiculatr to the running strand. The parallel structure isn't as strong howevre is still a very ridged structure.

Nnjm2 at 02:26, 29 November 2013

2013-11-29T02:26:21Z

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	~~== Overview ==~~

	The secondary structure of a protein describes the way in which a poly peptide chain of amino acids are folded.<br>These secondary structures can be separated into 2 section alpha-helicies and a beta-sheet formation, these describe the level of organisation of the specific foldin patterens.		The secondary structure of a protein describes the way in which a poly peptide chain of amino acids are folded.<br>These secondary structures can be separated into 2 section alpha-helicies and a beta-sheet formation, these describe the level of organisation of the specific foldin patterens.

	== ~~<br>~~Alpha-Helix ==		=== Alpha-Helix ===

	A alpha-helix is a right handed helix that resembles a right handed spiral staircase. An alpha helix contains hydrogen bonding between the N-H group of every peptide bond and C=O groups that are next to a peptide bond<ref>B.Alberts et al. (2014) Essencial Cell Biology 4th edition, Gartland Science, New York</ref>. these are usually loacated 4 amino acids away from each other but in the same chain. This is what produces the spiraling structure of the alpha-helix.		A alpha-helix is a right handed helix that resembles a right handed spiral staircase. An alpha helix contains hydrogen bonding between the N-H group of every peptide bond and C=O groups that are next to a peptide bond<ref>B.Alberts et al. (2014) Essencial Cell Biology 4th edition, Gartland Science, New York</ref>. these are usually loacated 4 amino acids away from each other but in the same chain. This is what produces the spiraling structure of the alpha-helix.

	The most common known helix structure is that of DNA, where 2 alpha helicies are wound around each other with complimentary base paring between them holding them together.		The most common known helix structure is that of DNA, where 2 alpha helicies are wound around each other with complimentary base paring between them holding them together.

	~~<br>~~		=== Beta-Sheet ===

	== Beta-Sheet ==

	The beta-sheet is where one chain of amino acids, form a parallel or antiparallel folded structure with hydrogen bonding between the ajacent strands of the fold, between N-H and C=O groups.<ref>B.Alberts et al. (2014) Essencial Cell Biology 4th edition, Gartland Science, New York</ref>		The beta-sheet is where one chain of amino acids, form a parallel or antiparallel folded structure with hydrogen bonding between the ajacent strands of the fold, between N-H and C=O groups.<ref>B.Alberts et al. (2014) Essencial Cell Biology 4th edition, Gartland Science, New York</ref>

	The antiparallel structure is stronger due to the almost perfect lining up of the strands to make hydrogen bonds that form directly perpendiculatr to the running strand. The parallel ~~structur~~ isn't as strong howevre is still a very ridged structure.		The antiparallel structure is stronger due to the almost perfect lining up of the strands to make hydrogen bonds that form directly perpendiculatr to the running strand. The parallel structure isn't as strong howevre is still a very ridged structure.

	== References ==		=== References ===

	<references />~~ ~~		<references />

120064290: Created page with "== Overview == The secondary structure of a protein describes the way in which a poly peptide chain of amino acids are folded.
These secondary structures can be separated in..."

2013-11-28T11:15:02Z

Created page with "== Overview == The secondary structure of a protein describes the way in which a poly peptide chain of amino acids are folded.<br>These secondary structures can be separated in..."

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== Overview ==

The secondary structure of a protein describes the way in which a poly peptide chain of amino acids are folded.<br>These secondary structures can be separated into 2 section alpha-helicies and a beta-sheet formation, these describe the level of organisation of the specific foldin patterens.

== <br>Alpha-Helix ==

A alpha-helix is a right handed helix that resembles a right handed spiral staircase. An alpha helix contains hydrogen bonding between the N-H group of every peptide bond and C=O groups that are next to a peptide bond<ref>B.Alberts et al. (2014) Essencial Cell Biology 4th edition, Gartland Science, New York</ref>. these are usually loacated 4 amino acids away from each other but in the same chain. This is what produces the spiraling structure of the alpha-helix.

The most common known helix structure is that of DNA, where 2 alpha helicies are wound around each other with complimentary base paring between them holding them together.

<br>

== Beta-Sheet ==

The beta-sheet is where one chain of amino acids, form a parallel or antiparallel folded structure with hydrogen bonding between the ajacent strands of the fold, between N-H and C=O groups.<ref>B.Alberts et al. (2014) Essencial Cell Biology 4th edition, Gartland Science, New York</ref>

The antiparallel structure is stronger due to the almost perfect lining up of the strands to make hydrogen bonds that form directly perpendiculatr to the running strand. The parallel structur isn't as strong howevre is still a very ridged structure.

== References ==

<references /> 