Document Detail


Collective Variable Description of Native Protein Dynamics.
MedLine Citation:
PMID:  24329489     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
The importance of collective motions in proteins, such as hinge-bending motions or motions involving domains, has been recognized. Occurrence of such motions and their experimental and theoretical studies are reviewed. Normal-mode analysis and principal component analysis are powerful theoretical tools for studying such motions. The former is based on the assumption of harmonicity of the dynamics, while the latter is valid even when the dynamics is highly anharmonic. The results of the latter analysis indicate that most important conformational events are taking place in a conformational subspace spanned by a rather small number of principal modes, and this important subspace is also spanned by a small number of normal modes. The normal-mode refinement method of protein X-ray crystallography, which is developed based on the concept of the above important subspace, is discussed.
Authors:
Steven Hayward; Nobuhiro Go
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Publication Detail:
Type:  JOURNAL ARTICLE    
Journal Detail:
Title:  Annual review of physical chemistry     Volume:  46     ISSN:  1545-1593     ISO Abbreviation:  Annu Rev Phys Chem     Publication Date:  1995 Oct 
Date Detail:
Created Date:  2013-12-16     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  15040080R     Medline TA:  Annu Rev Phys Chem     Country:  -    
Other Details:
Languages:  ENG     Pagination:  223-250     Citation Subset:  -    
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