Membrane protein folding and stability: physical principles.

阅读量：

166

作者：

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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.

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关键词：

lipid-protein interactions, peptide-bilayer interactions, membrane-active peptides, antimicrobial peptides, thermodynamics, bilayer structure, soluble protein folding

DOI：

10.1146/annurev.biophys.28.1.319

被引量：

2856

年份：

1999