Document Detail


Comparing bound and unbound protein structures using energy calculation and rotamer statistics.
MedLine Citation:
PMID:  12542419     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Protein data in the PDB covers only a snapshot of a protein structure. For flexible docking conformational changes need to be considered. Rotamer statistics provide the likelihood for side chain conformations, and further comparison of bound and unbound state yields differences in preferred positions. Furthermore, we do a full sampling of selected chi angles and apply the AMBER force field. Conformation of energy minima complies with the rotamer statistics. Both types of information target the reduction of search space for enumerative docking algorithms and provide parameters for elastic docking.
Authors:
Kerstin Koch; Frank Zöllner; Steffen Neumann; Franz Kummert; Gerhard Sagerer
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  In silico biology     Volume:  2     ISSN:  1386-6338     ISO Abbreviation:  In Silico Biol. (Gedrukt)     Publication Date:  2002  
Date Detail:
Created Date:  2003-01-28     Completed Date:  2003-07-17     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9815902     Medline TA:  In Silico Biol     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  351-68     Citation Subset:  IM    
Affiliation:
Technische Fakultät, AG Angewandte Informatik, Universität Bielefeld, Postfach 100131, 33501 Bielefeld, Germany. kerstin@techfak.uni-bielefeld.de
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MeSH Terms
Descriptor/Qualifier:
Databases, Protein
Protein Binding
Protein Conformation
Proteins / chemistry*,  metabolism
Chemical
Reg. No./Substance:
0/Proteins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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