Folding and stability of integral membrane proteins in amphipols

Jörg H Kleinschmidt; Jean-Luc Popot

doi:10.1016/j.abb.2014.10.013

Folding and stability of integral membrane proteins in amphipols

Arch Biochem Biophys. 2014 Dec 15:564:327-43. doi: 10.1016/j.abb.2014.10.013. Epub 2014 Oct 30.

Authors

Jörg H Kleinschmidt¹, Jean-Luc Popot²

Affiliations

¹ Abteilung Biophysik, Institut für Biologie, FB 10, Universität Kassel and Center for Interdisciplinary Nanostructure Science and Technology (CINSaT), Heinrich-Plett-Str. 40, D-34132 Kassel, Germany. Electronic address: jhk@uni-kassel.de.
² Laboratoire de Physico-Chimie Moléculaire des Protéines Membranaires, UMR 7099, Centre National de la Recherche Scientifique/Université Paris-7, Institut de Biologie Physico-Chimique (FRC 550), 13, rue Pierre-et-Marie-Curie, F-75005 Paris, France. Electronic address: jean-luc.popot@ibpc.fr.

PMID: 25449655
DOI: 10.1016/j.abb.2014.10.013

Abstract

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.

Keywords: A8-35; Amphipols; Bacteriorhodopsin; Folding; G protein-coupled receptors; Kinetics; Membrane protein; Outer membrane proteins; Thermodynamic stability.

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

Detergents / chemistry*
Membrane Proteins / chemistry*
Protein Denaturation*
Protein Folding*
Protein Stability
Solubility

Substances

Detergents
Membrane Proteins