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Dynamics based alignment of proteins: an alternative approach to quantify dynamic similarity.

Abstract:

BACKGROUND: The dynamic motions of many proteins are central to their function. It therefore follows that the dynamic requirements of a protein are evolutionary constrained. In order to assess and quantify this, one needs to compare the dynamic motions of different proteins. Comparing the dynamics of distinct proteins may also provide insight into how protein motions are modified by variations in sequence and, consequently, by structure. The optimal way of comparing complex molecular motions...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1186/1471-2105-11-188

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Institution:
University of Oxford
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Statistics
Role:
Author
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Institution:
University of Oxford
Division:
MPLS
Department:
Statistics
Role:
Author
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Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
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Name:
Polygene
Grant:
LSHC-CT-2005-018827
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Name:
Research Councils UK
Funding agency for:
Biggin, P
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Name:
National Institutes of Health
Publisher:
BioMed Central
Journal:
BMC bioinformatics More from this journal
Volume:
11
Issue:
1
Pages:
188
Publication date:
2010-04-14
DOI:
EISSN:
1471-2105
ISSN:
1471-2105
Language:
English
Keywords:
UUID:
uuid:8a3dadeb-9e15-4104-a7f9-c6f9c38f6bba
Local pid:
pubs:100068
Source identifiers:
100068
Deposit date:
2012-12-19

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