Membrane Protein Structures in Lipid Bilayers; Small-Angle Neutron Scattering With Contrast-Matched Bicontinuous Cubic Phases
Conn, Charlotte E. ; de Campo, Liliana ; Whitten, Andrew E. ; Garvey, Christopher J. LU
; Krause-Heuer, Anwen M.
and van 't Hag, Leonie
(2021)
In Frontiers in Chemistry
8.
- Abstract
This perspective describes advances in determining membrane protein structures in lipid bilayers using small-angle neutron scattering (SANS). Differentially labeled detergents with a homogeneous scattering length density facilitate contrast matching of detergent micelles; this has previously been used successfully to obtain the structures of membrane proteins. However, detergent micelles do not mimic the lipid bilayer environment of the cell membrane in vivo. Deuterated vesicles can be used to obtain the radius of gyration of membrane proteins, but protein-protein interference effects within the vesicles severely limits this method such that the protein structure cannot be modeled. We show herein that different membrane protein... (More)
This perspective describes advances in determining membrane protein structures in lipid bilayers using small-angle neutron scattering (SANS). Differentially labeled detergents with a homogeneous scattering length density facilitate contrast matching of detergent micelles; this has previously been used successfully to obtain the structures of membrane proteins. However, detergent micelles do not mimic the lipid bilayer environment of the cell membrane in vivo. Deuterated vesicles can be used to obtain the radius of gyration of membrane proteins, but protein-protein interference effects within the vesicles severely limits this method such that the protein structure cannot be modeled. We show herein that different membrane protein conformations can be distinguished within the lipid bilayer of the bicontinuous cubic phase using contrast-matching. Time-resolved studies performed using SANS illustrate the complex phase behavior in lyotropic liquid crystalline systems and emphasize the importance of this development. We believe that studying membrane protein structures and phase behavior in contrast-matched lipid bilayers will advance both biological and pharmaceutical applications of membrane-associated proteins, biosensors and food science.
(Less)
- author
- Conn, Charlotte E.
; de Campo, Liliana
; Whitten, Andrew E.
; Garvey, Christopher J.
LU
; Krause-Heuer, Anwen M.
and van 't Hag, Leonie
- organization
- publishing date
- 2021
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- lipid cubic phase, membrane protein, peptide structure, self-assembly, small-angle scattering
- in
- Frontiers in Chemistry
- volume
- 8
- article number
- 619470
- publisher
- Frontiers Media S. A.
- external identifiers
-
- scopus:85101679931
- pmid:33644002
- ISSN
- 2296-2646
- DOI
- 10.3389/fchem.2020.619470
- language
- English
- LU publication?
- yes
- id
- cc29858e-69d6-4fe7-8208-87df57c2acfa
- date added to LUP
- 2021-03-15 13:45:53
- date last changed
- 2024-06-13 08:33:17
@article{cc29858e-69d6-4fe7-8208-87df57c2acfa,
abstract = {{<p>This perspective describes advances in determining membrane protein structures in lipid bilayers using small-angle neutron scattering (SANS). Differentially labeled detergents with a homogeneous scattering length density facilitate contrast matching of detergent micelles; this has previously been used successfully to obtain the structures of membrane proteins. However, detergent micelles do not mimic the lipid bilayer environment of the cell membrane in vivo. Deuterated vesicles can be used to obtain the radius of gyration of membrane proteins, but protein-protein interference effects within the vesicles severely limits this method such that the protein structure cannot be modeled. We show herein that different membrane protein conformations can be distinguished within the lipid bilayer of the bicontinuous cubic phase using contrast-matching. Time-resolved studies performed using SANS illustrate the complex phase behavior in lyotropic liquid crystalline systems and emphasize the importance of this development. We believe that studying membrane protein structures and phase behavior in contrast-matched lipid bilayers will advance both biological and pharmaceutical applications of membrane-associated proteins, biosensors and food science.</p>}},
author = {{Conn, Charlotte E. and de Campo, Liliana and Whitten, Andrew E. and Garvey, Christopher J. and Krause-Heuer, Anwen M. and van 't Hag, Leonie}},
issn = {{2296-2646}},
keywords = {{lipid cubic phase; membrane protein; peptide structure; self-assembly; small-angle scattering}},
language = {{eng}},
publisher = {{Frontiers Media S. A.}},
series = {{Frontiers in Chemistry}},
title = {{Membrane Protein Structures in Lipid Bilayers; Small-Angle Neutron Scattering With Contrast-Matched Bicontinuous Cubic Phases}},
url = {{http://dx.doi.org/10.3389/fchem.2020.619470}},
doi = {{10.3389/fchem.2020.619470}},
volume = {{8}},
year = {{2021}},
}