Folding and stability of integral membrane proteins in amphipols

被引：32
|
作者：
Kleinschmidt, Joerg H. [1 ,2 ]
Popot, Jean-Luc [3 ]
机构：
[1] Univ Kassel, Inst Biol, Biophys Abt, D-34132 Kassel, Germany
[2] Ctr Interdisciplinary Nanostruct Sci & Technol CI, D-34132 Kassel, Germany
[3] Univ Paris 07, CNRS, Inst Biol Phys Chim FRC 550, Lab Phys Chim Mol Prot Membranaires,UMR 7099, F-75005 Paris, France
来源：
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 2014年 / 564卷
基金：
美国国家卫生研究院;
关键词：
Membrane protein; Folding; Amphipols; Kinetics; Thermodynamic stability; Outer membrane proteins; Bacteriorhodopsin; G protein-coupled receptors; A8-35; MOLECULAR-DYNAMICS SIMULATIONS; THERMALLY-INDUCED AGGREGATION; RESONANCE ENERGY-TRANSFER; BETA-BARREL PROTEINS; CELL-FREE SYNTHESIS; OUTER-MEMBRANE; ESCHERICHIA-COLI; LIPID-BILAYERS; IN-VITRO; SARCOPLASMIC-RETICULUM;
D O I：
10.1016/j.abb.2014.10.013
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：
Amphipols (APols) are a family of amphipathic polymers designed to keep transmembrane proteins (TMPs) soluble in aqueous solutions in the absence of detergent. APols have proven remarkably efficient at (i) stabilizing TMPs, as compared to detergent solutions, and (ii) folding them from a denatured state to a native, functional one. The underlying physical chemical mechanisms are discussed. (C) 2014 Elsevier Inc. All rights reserved.
引用
收藏
页码：327 / 343
页数：17
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