Synthetic peptides as models for intrinsic membrane proteins

被引：129

作者：

Killian, JA ^{[1
]}

机构：

[1] Univ Utrecht, Dept Membrane Biochem, Ctr Biomembranes & Lipid Enzymol, Inst Biomembranes, NL-3584 CH Utrecht, Netherlands

来源：

FEBS LETTERS | 2003年 / 555卷 / 01期

关键词：

transmembrane peptide; alpha-helix; hydrophobic mismatch; interfacial anchoring; snorkeling; tryptophan;

D O I：

10.1016/S0014-5793(03)01154-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

There are many ways in which lipids can modulate the activity of membrane proteins. Simply a change in hydrophobic thickness of the lipid bilayer, for example, already can have various consequences for membrane protein organization and hence for activity. By using synthetic transmembrane peptides, it could be established that these consequences include peptide oligomerization, tilt of transmembrane segments, and reorientation of side chains, depending on the specific properties of the peptides and lipids used. The results illustrate the potential of the use of synthetic model peptides to establish general principles that govern interactions between membrane proteins and surrounding lipids. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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收藏

页码：134 / 138

页数：5

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