Biochemistry of the glycosyl-phosphatidylinositol membrane protein anchors.
Biochemistry of the glycosyl-phosphatidylinositol membrane protein anchors.
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DOI:
10.1042/bj2440001
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发表时间:
1987-05
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影响因子:
--
通讯作者:
Martin G. Low
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文献类型:
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作者:
Martin G. Low
1. Introduction (a) Anchoring of membrane proteins. It is generally accepted that the predominant structural feature of most biological membranes is a lipid bilayer with proteins either bound to the polar surface or penetrating the bilayer interior to some extent. The net force which holds the latter group of proteins (ie, integral membrane proteins) in the membrane is the balance of interactions between relatively hydrophobic and polar polypeptide domains with the hydrophobic core of the lipid bilayer and the surrounding medium, respectively (Capaldi, 1982; Singer & Nicolson, 1972). These forces are not only important for attaching these proteins to the membrane, but also permit the protein to adopt its correct conformation and transmembrane orientation so that its function (ie solute transport, signal transduction, adhesion, etc.) can be performed correctly. Membrane proteins vary markedly in the nature and (a)(b)(c)