Membrane protein folding and stability: Physical principles

被引:1466
作者
White, SH [1 ]
Wimley, WC
机构
[1] Univ Calif Irvine, Dept Physiol & Biophys, Irvine, CA 92697 USA
[2] Tulane Univ, Med Ctr, Dept Biochem, New Orleans, LA 70112 USA
来源
ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE | 1999年 / 28卷
关键词
lipid-protein interactions; peptide-bilayer interactions; membrane-active peptides; antimicrobial peptides; thermodynamics; bilayer structure; soluble protein folding;
D O I
10.1146/annurev.biophys.28.1.319
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
Stably folded membrane proteins reside in a free energy minimum determined by the interactions of the peptide chains with each other, the lipid bilayer hydrocarbon core, the bilayer interface, and with water. The prediction of three-dimensional structure from sequence requires a detailed understanding of these interactions. Progress toward this objective is summarized in this review by means of a thermodynamic framework for describing membrane protein folding and stability. The framework includes a coherent thermodynamic formalism for determining and describing the energetics of peptide-bilayer interactions and a review of the properties of the environment of membrane proteins-the bilayer milieu. Using a four-step thermodynamic cycle as a guide, advances in three main aspects of membrane protein folding energetics are discussed: protein binding and folding in bilayer interfaces, transmembrane helix insertion, and helix-helix interactions. The concepts of membrane protein stability that emerge provide insights to fundamental issues of protein folding.
引用
收藏
页码:319 / 365
页数:47
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