Issue 43, 2021

Towards a native environment: structure and function of membrane proteins in lipid bilayers by NMR

Abstract

Solid-state NMR (ssNMR) is a versatile technique that can be used for the characterization of various materials, ranging from small molecules to biological samples, including membrane proteins. ssNMR can probe both the structure and dynamics of membrane proteins, revealing protein function in a near-native lipid bilayer environment. The main limitation of the method is spectral resolution and sensitivity, however recent developments in ssNMR hardware, including the commercialization of 28 T magnets (1.2 GHz proton frequency) and ultrafast MAS spinning (<100 kHz) promise to accelerate acquisition, while reducing sample requirement, both of which are critical to membrane protein studies. Here, we review recent advances in ssNMR methodology used for structure determination of membrane proteins in native and mimetic environments, as well as the study of protein functions such as protein dynamics, and interactions with ligands, lipids and cholesterol.

Graphical abstract: Towards a native environment: structure and function of membrane proteins in lipid bilayers by NMR

Article information

Article type
Perspective
Submitted
24 Maijs 2021
Accepted
07 Sept. 2021
First published
07 Sept. 2021
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY license

Chem. Sci., 2021,12, 14332-14342

Towards a native environment: structure and function of membrane proteins in lipid bilayers by NMR

K. Xue, K. T. Movellan, X. C. Zhang, E. E. Najbauer, M. C. Forster, S. Becker and L. B. Andreas, Chem. Sci., 2021, 12, 14332 DOI: 10.1039/D1SC02813H

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

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