Neutron reflectometry (NR) is a large-facility technique used to examine structure at interfaces. In this brief review an introduction to the utilisation of NR in the study of protein–lipid interactions is given. Cold neutron beams penetrate matter deeply, have low energies, wavelengths in the Ångstrom regime and are sensitive to light elements. High differential hydrogen sensitivity (between protium and deuterium) enables solution and sample isotopic labelling to be utilised to enhance or diminish the scattering signal of individual components within complex biological structures. The combination of these effects means NR can probe buried structures such as those at the solid–liquid interface and encode molecular level structural information on interfacial protein–lipid complexes revealing the relative distribution of components as well as the overall structure. Model biological membrane sample systems can be structurally probed to examine phenomena such as antimicrobial mode of activity, as well as structural and mechanistic properties peripheral/integral proteins within membrane complexes. Here, the example of the antimicrobial protein α1-purothionin binding to a model Gram negative bacterial outer membrane is used to highlight the utilisation of this technique, detailing how changes in the protein/lipid distributions across the membrane before and after the protein interaction can be easily encoded using hydrogen isotope labelling.
Skip Nav Destination
Article navigation
August 2021
-
Cover Image
Cover Image
Glycoproteomics is the tool of choice in glycobiology to decipher the role of protein glycosylation in health and disease in a system-wide context for integration into multi-omics studies. For a hitchhiker's guide to glcoproteomics, see the review by Oliveira and colleagues (pp. 1623–1642). Cover artwork provided by Daniel Kolarich.
Review Article|
July 09 2021
Unravelling the structural complexity of protein–lipid interactions with neutron reflectometry
Luke A. Clifton
ISIS Pulsed Neutron and Muon Source, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Harwell Science and Innovation Campus, Didcot, Oxfordshire OX11 OQX, U.K.
Correspondence: Luke A. Clifton ([email protected])
Search for other works by this author on:
Publisher: Portland Press Ltd
Received:
March 18 2021
Revision Received:
June 02 2021
Accepted:
June 14 2021
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2021 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society
2021
Biochem Soc Trans (2021) 49 (4): 1537–1546.
Article history
Received:
March 18 2021
Revision Received:
June 02 2021
Accepted:
June 14 2021
Citation
Luke A. Clifton; Unravelling the structural complexity of protein–lipid interactions with neutron reflectometry. Biochem Soc Trans 27 August 2021; 49 (4): 1537–1546. doi: https://doi.org/10.1042/BST20201071
Download citation file:
Sign in
Don't already have an account? Register
Sign in to your personal account
You could not be signed in. Please check your email address / username and password and try again.
Could not validate captcha. Please try again.
Biochemical Society Member Sign in
Sign InSign in via your Institution
Sign in via your InstitutionGet Access To This Article
Cited By
Get Email Alerts
Open Access for all
We offer compliant routes for all authors from 2025. With library support, there will be no author nor reader charges in 5 journals. Check here |
![]() |