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Updated: Apr 20, 2026

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
Published on: April 28, 2011
Folding and stability of integral membrane proteins in amphipols
Jörg H Kleinschmidt1, Jean-Luc Popot2
1Abteilung 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.
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.
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