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Combined 1H-Detected Solid-State NMR.pdf (6.17 MB)

Combined 1H-Detected solid-state NMR spectroscopy and electron cryotomography to study membrane proteins across resolutions in native environments

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posted on 2023-06-09, 09:07 authored by Lindsay A Baker, Tessa Sinnige, Pascale Schellenberger, Jeanine de Keyzer, C Alistair Siebert, Arnold J M Driessen, Marc Baldus, Kay Grünewald
Membrane proteins remain challenging targets for structural biology, despite much effort, as their native environment is heterogeneous and complex. Most methods rely on detergents to extract membrane proteins from their native environment, but this removal can significantly alter the structure and function of these proteins. Here, we overcome these challenges with a hybrid method to study membrane proteins in their native membranes, combining high-resolution solid-state nuclear magnetic resonance spectroscopy and electron cryotomography using the same sample. Our method allows the structure and function of membrane proteins to be studied in their native environments, across different spatial and temporal resolutions, and the combination is more powerful than each technique individually. We use the method to demonstrate that the bacterial membrane protein YidC adopts a different conformation in native membranes and that substrate binding to YidC in these native membranes differs from purified and reconstituted systems

History

Publication status

  • Published

File Version

  • Published version

Journal

Structure

ISSN

0969-2126

Publisher

Elsevier

Issue

1

Volume

26

Page range

161-170

Department affiliated with

  • Biochemistry Publications

Full text available

  • Yes

Peer reviewed?

  • Yes

Legacy Posted Date

2018-03-08

First Open Access (FOA) Date

2018-03-13

First Compliant Deposit (FCD) Date

2018-03-12

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