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Author(s): White SH; Wimley WC
Title: Membrane protein folding and stability: Physical principles
Source: ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE 28: 319-365
Date: 1999
Document Type: Journal : Review
DOI:
Language: English
Comment:
Address: Univ Calif Irvine, Dept Physiol & Biophys, Irvine, CA 92697 USA.
Tulane Univ, Med Ctr, Dept Biochem, New Orleans, LA 70112 USA. Reprint: White, SH, Univ Calif Irvine, Dept Physiol & Biophys, Irvine, CA 92697
USA. E-mail:
Author Keywords: lipid-protein interactions; peptide-bilayer interactions; membrane-
active peptides; antimicrobial peptides; thermodynamics; bilayer
structure; soluble protein folding
KeyWords Plus: PHOTOSYNTHETIC REACTION CENTER; TRANSMEMBRANE ALPHA-HELICES; LIGHT-
HARVESTING COMPLEX; CYTOCHROME-C-OXIDASE; EXPRESSED POLYPEPTIDE
FRAGMENTS; BILAYER STRUCTURE DETERMINATION; PHOSPHOLIPID MODEL
MEMBRANE; GLYCOPHORIN-A DIMERIZATION; AMINO-ACID-RESIDUES; X-RAY-
DIFFRACTION
Abstract: 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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