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	<updated>2026-04-14T23:40:18Z</updated>
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		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Integral_and_peripheral_membrane_proteins&amp;diff=23418</id>
		<title>Integral and peripheral membrane proteins</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Integral_and_peripheral_membrane_proteins&amp;diff=23418"/>
		<updated>2018-12-09T20:48:26Z</updated>

		<summary type="html">&lt;p&gt;180596106: added missing information and attached a picture showing the content of the page&lt;/p&gt;
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&lt;div&gt;=== Integral Membrane Proteins  ===&lt;br /&gt;
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These are [[Protein|proteins]] directly linked to the [[Plasma membrane|plasma membrane]] of [[Cells|cells]]. They are also considered as proteins that fully pass through the membrane ([[Carrier proteins|carrier proteins]] and [[Channel proteins|channel proteins]]). Transmembrane proteins can be single-pass, (pass through the membrane once), or mulitpass (pass through the membrane more than once). These [[Transmembrane proteins|transmembrane proteins]] have both [[Hydrophillic|hydrophilic]] and [[Hydrophobic|hydrophobic]] regions; they are [[Amphiphilic|amphiphilic]]&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, Pages 629-630, New York: Garland Science&amp;lt;/ref&amp;gt;. The hydrophobic regions are the regions inside the lipid membrane, so they are kept away from water, whereas the hydrophilic regions are on either side of the membrane&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, Pages 630, New York: Garland Science&amp;lt;/ref&amp;gt;. The hydrophobic regions interact with the hydrophobic tails on [[Phospholipid|lipids]] inside the membrane. The transmembrane domains are usually made up of [[Alpha-helix|alpha-helices]], although can be made up of [[Beta-sheet|beta-sheets]] rolled up into a [[Beta Barrel|beta-barrell]]. &lt;br /&gt;
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There is also a group of proteins that do not cross the lipid bilayer but are attached to only one side of it. That can be because: &lt;br /&gt;
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*they have a hydrophobic segment that can dive into the [https://teaching.ncl.ac.uk/bms/wiki/index.php/Phospholipid phospholipid] layer &lt;br /&gt;
*they are attached [https://teaching.ncl.ac.uk/bms/wiki/index.php/Covalent covalently] to lipids of the bilayer &lt;br /&gt;
*they are bind via an [https://teaching.ncl.ac.uk/bms/wiki/index.php/Oligosaccharide oligosaccharide] linker(covalent interactions)&amp;lt;ref&amp;gt;Alberts B et al. Molecular Biology of the Cell. 6th ed., New York: Garland Science, Taylor &amp;amp;amp;amp;amp;amp;amp;amp;amp;amp; Francis group, LLC. 2015&amp;lt;/ref&amp;gt;&lt;br /&gt;
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They do not readily disocciate with the cell membrane, and&amp;amp;nbsp;can therefore only be separated from the plasma membrane through the&amp;amp;nbsp;use of detergents (and other agents) to disrupt the plasma membrane. &lt;br /&gt;
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=== Peripheral Membrane Proteins  ===&lt;br /&gt;
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These proteins are connected to the plasma membrane through intermediate [[Molecules|molecules]] (even integral proteins) by [https://teaching.ncl.ac.uk/bms/wiki/index.php/Noncovalent_bonds noncovalent ]interactions. They are released from the plasma membrane by agents that disrupts protein-protein interactions, e.g. by simply increasing the salt concentration of the buffer solution which the cells are suspended in.&amp;lt;br&amp;gt; &lt;br /&gt;
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=== Membrane proteins association with lipid bilayer  ===&lt;br /&gt;
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====== [[Image:Membrane proteins and lipid bilayer.png|frame|left]]Figure 1. Various ways in which proteins associate with the lipid bilayer&amp;lt;ref&amp;gt;Alberts B et al. Molecular Biology of the Cell. 6th ed., New York: Garland Science, Taylor &amp;amp;amp;amp;amp;amp;amp;amp;amp; Francis group, LLC. 2015&amp;lt;/ref&amp;gt;  ======&lt;br /&gt;
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#&amp;lt;span style=&amp;quot;font-size: 13.28px;&amp;quot;&amp;gt;single&amp;amp;nbsp; α-helix&amp;lt;/span&amp;gt; &lt;br /&gt;
#multiple&amp;amp;nbsp; α-helices &lt;br /&gt;
#β-barrel &lt;br /&gt;
#association by a hydrophobic face of the&amp;amp;nbsp;α-helix &lt;br /&gt;
#attached to a lipid &lt;br /&gt;
#attached via oligosaccharide linker &lt;br /&gt;
#8. membrane-associated proteins&lt;br /&gt;
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===  ===&lt;br /&gt;
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===  ===&lt;br /&gt;
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====== &amp;lt;br&amp;gt;  ======&lt;br /&gt;
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====== &amp;lt;br&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>180596106</name></author>
	</entry>
	<entry>
		<id>https://teaching.ncl.ac.uk/bms/wiki//index.php?title=File:Membrane_proteins_and_lipid_bilayer.png&amp;diff=23408</id>
		<title>File:Membrane proteins and lipid bilayer.png</title>
		<link rel="alternate" type="text/html" href="https://teaching.ncl.ac.uk/bms/wiki//index.php?title=File:Membrane_proteins_and_lipid_bilayer.png&amp;diff=23408"/>
		<updated>2018-12-09T20:25:51Z</updated>

		<summary type="html">&lt;p&gt;180596106: Membrane proteins association with lipid bilayer&lt;/p&gt;
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&lt;div&gt;Membrane proteins association with lipid bilayer&lt;/div&gt;</summary>
		<author><name>180596106</name></author>
	</entry>
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