- Abstract:
-
Chemical crosslinking can identify the neighborhood relationships between specific amino-acid residues in proteins. The interpretation of crosslinking data is typically performed using single, static atomic structures. However, proteins are dynamic, undergoing motions spanning from local fluctuations of individual residues to global motions of protein assemblies. Here we demonstrate that failure to explicitly accommodate dynamics when interpreting crosslinks structurally can lead to considera...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Accepted Manuscript
- Files:
-
-
(pdf, 8.8MB)
-
- Publisher copy:
- 10.1016/j.str.2017.08.015
-
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- Grant:
- Impact Acceleration Awards (to J.L.P.B.) BB/IAA/Oxford/15
- Publisher:
- Cell Press Publisher's website
- Journal:
- Structure Journal website
- Volume:
- 25
- Issue:
- 11
- Pages:
- 1751-1757.e5
- Publication date:
- 2018-09-28
- Acceptance date:
- 2017-08-28
- DOI:
- EISSN:
-
1878-4186
- ISSN:
-
0969-2126
- Pubs id:
-
pubs:732945
- URN:
-
uri:99c2c988-cbaa-4764-b0e8-d1ed6ee17fdb
- UUID:
-
uuid:99c2c988-cbaa-4764-b0e8-d1ed6ee17fdb
- Local pid:
- pubs:732945
- Paper number:
- 11
- Language:
- English
- Keywords:
- Copyright holder:
- Elsevier Ltd
- Copyright date:
- 2018
- Notes:
-
Copyright © 2017 Elsevier Ltd. This is the accepted manuscript version of the article. The final version is available online from Cell Press at: https://doi.org/10.1016/j.str.2017.08.015
Journal article
Accommodating protein dynamics in the modeling of chemical crosslinks
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