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.

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