Journal article
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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(Version of record, pdf, 2.8MB)
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- Publisher copy:
- 10.1186/1471-2105-11-188
Authors
Funding
National Institutes of Health
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John Fell Fund
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Wellcome Trust
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Bibliographic Details
- Publisher:
- BioMed Central Publisher's website
- Journal:
- BMC bioinformatics Journal website
- Volume:
- 11
- Issue:
- 1
- Pages:
- 188
- Publication date:
- 2010-04-14
- DOI:
- EISSN:
-
1471-2105
- ISSN:
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1471-2105
Item Description
- Language:
- English
- Keywords:
- UUID:
-
uuid:8a3dadeb-9e15-4104-a7f9-c6f9c38f6bba
- Local pid:
- pubs:100068
- Source identifiers:
-
100068
- Deposit date:
- 2012-12-19
Terms of use
- Copyright holder:
- Münz et al
- Copyright date:
- 2010
- Notes:
- © 2010 Münz et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
- Licence:
- CC Attribution (CC BY)
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