Abstract
How alpha-helical membrane proteins fold correctly in the highly hydrophobic membrane interior is not well understood. Their folding is known to be highly influenced by the lipids within the surrounding bilayer, but the majority of folding studies have focused on detergent-solubilized protein rather than protein in a lipid environment. There are different ways to study folding in lipid bilayers, and each method has its own advantages and disadvantages. This review will discuss folding methods which can be used to study alpha-helical membrane proteins in bicelles, liposomes, nanodiscs or native membranes. These folding methods include in vitro folding methods in liposomes such as denaturant unfolding studies, and single-molecule force spectroscopy studies in bicelles, liposomes and native membranes. This review will also discuss recent advances in co-translational folding studies, which use cell-free expression with liposomes or nanodiscs or are performed in vivo with native membranes.
| Original language | English |
|---|---|
| Article number | 220054 |
| Number of pages | 14 |
| Journal | Open Biology |
| Volume | 12 |
| Issue number | 7 |
| Early online date | 20 Jul 2022 |
| DOIs | |
| Publication status | E-pub ahead of print - 20 Jul 2022 |
Bibliographical note
Copyright © 2022 The Authors. Published by the Royal Society under the terms of the Creative Commons Attribution License https://creativecommons.org/licenses/by/4.0/, which permits unrestricted use, provided the original author and source are credited.Funding
We acknowledge funding from the European Research Council, ERC Advanced grant no. 294342 and Wellcome Trust Investigator Award 214259/Z/18/Z to P.J.B., King's College London for a PhD studentship for L.R.B., and King's College London and the Francis Crick Institute for a PhD studentship for S.G.-B.