Transmembrane domains: Difference between revisions
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Transmembrane domains are stretches of residues of integral membrane proteins that span across the membrane bilayer. They are key in a wide range of integral membrane proteins including receptors for [[Growth factors]] and [[Hormones]], channel proteins and two-way membrane transporters. Most transmembrane domains span the membrane 1-17 times, the most common being 1, 4 or 7 ([[G-protein linked receptor]] for example) <ref>http://www.els.net/WileyCDA/ElsArticle/refId-a0005051.html</ref>. | Transmembrane domains are stretches of residues of integral membrane proteins that span across the membrane bilayer. They are key in a wide range of integral membrane proteins including receptors for [[Growth factors]] and [[Hormones]], [[Channel_proteins|channel proteins ]]and two-way membrane transporters. Most transmembrane domains span the membrane 1-17 times, the most common being 1, 4 or 7 ([[G-protein linked receptor]] for example) <ref>http://www.els.net/WileyCDA/ElsArticle/refId-a0005051.html</ref>. | ||
=== References === | === References === | ||
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Revision as of 16:28, 4 December 2016
Transmembrane domains are stretches of residues of integral membrane proteins that span across the membrane bilayer. They are key in a wide range of integral membrane proteins including receptors for Growth factors and Hormones, channel proteins and two-way membrane transporters. Most transmembrane domains span the membrane 1-17 times, the most common being 1, 4 or 7 (G-protein linked receptor for example) [1].