- Abstract:
-
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 reson...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Publisher's version
- Files:
-
-
(pdf, 6.9MB)
-
- Publisher copy:
- 10.1016/j.str.2017.11.011
-
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- Grant:
- 700.26.121 and 700.10.443 to M.B.
- Publisher:
- Cell Press Publisher's website
- Journal:
- Structure Journal website
- Volume:
- 26
- Issue:
- 1
- Pages:
- 161-170.e3
- Publication date:
- 2017-12-14
- Acceptance date:
- 2017-11-15
- DOI:
- EISSN:
-
1878-4186
- ISSN:
-
0969-2126
- Pubs id:
-
pubs:813191
- URN:
-
uri:0d5344b8-4fde-4ff2-b7a7-3d81f5e584dc
- UUID:
-
uuid:0d5344b8-4fde-4ff2-b7a7-3d81f5e584dc
- Local pid:
- pubs:813191
- Language:
- English
- Keywords:
- Copyright holder:
- Baker et al.
- Copyright date:
- 2017
- Notes:
-
Copyright © 2017 The Authors. Published by Elsevier Ltd. 161
This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
Journal article
Combined 1H-detected solid-state NMR spectroscopy and electron cryotomography to study membrane proteins across resolutions in native environments
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