Methods to study folding of alpha-helical membrane proteins in lipids

Nicola J. Harris; Grant A. Pellowe; Laura R. Blackholly; Samuel Gulaidi-Breen; Heather E. Findlay; Paula J. Booth

doi:10.1098/rsob.220054

Methods to study folding of alpha-helical membrane proteins in lipids

Nicola J. Harris^*, Grant A. Pellowe, Laura R. Blackholly, Samuel Gulaidi-Breen, Heather E. Findlay, Paula J. Booth

^*Corresponding author for this work

Francis Crick Institute

Research output: Contribution to journal › Review article › peer-review

9 Citations (Scopus)

117 Downloads (Pure)

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
Journal	Open Biology
Volume	12
Issue number	7
DOIs	https://doi.org/10.1098/rsob.220054
Publication status	Published - 20 Jul 2022

Keywords

folding
lipids
membrane
protein

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10.1098/rsob.220054Licence: CC BY

Methods to study folding_HARRIS_Publishedonline20July2022_GOLD VoR (CC BY)Final published version, 1.62 MBLicence: CC BY

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title = "Methods to study folding of alpha-helical membrane proteins in lipids",

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. ",

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author = "Harris, {Nicola J.} and Pellowe, {Grant A.} and Blackholly, {Laura R.} and Samuel Gulaidi-Breen and Findlay, {Heather E.} and Booth, {Paula J.}",

note = "Funding Information: 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. Publisher Copyright: {\textcopyright} ",

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AU - Blackholly, Laura R.

AU - Gulaidi-Breen, Samuel

AU - Findlay, Heather E.

AU - Booth, Paula J.

N1 - Funding Information: 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. Publisher Copyright: ©

PY - 2022/7/20

Y1 - 2022/7/20

N2 - 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.

AB - 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.

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Methods to study folding of alpha-helical membrane proteins in lipids

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