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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
Version:
Accepted Manuscript

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Publisher copy:
10.1016/j.str.2017.08.015

Authors


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Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry; Physical & Theoretical Chem
Oxford college:
University College
Role:
Author
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Grant:
Impact Acceleration Awards (to J.L.P.B.) BB/IAA/Oxford/15
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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
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

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