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Accommodating protein dynamics in the modeling of chemical crosslinks

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...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1016/j.str.2017.08.015

Authors


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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Physical & Theoretical Chem
Oxford college:
University College
Role:
Author
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Grant:
BBSRC David Phillips Fellowship (BB/J014346/1 to A.J.B.
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Grant:
University Research Fellowship (UF120251 to J.L.P.B.
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
Pmid:
28966018
Source identifiers:
732945
Language:
English
Keywords:
Pubs id:
pubs:732945
UUID:
uuid:99c2c988-cbaa-4764-b0e8-d1ed6ee17fdb
Local pid:
pubs:732945
Deposit date:
2017-11-01

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