Collective protein dynamics in relation to function.
Several techniques for the analysis of the internal motions of proteins are available - separating large collective motions from small, presumably uninteresting motions. Such descriptions are helpful in the characterization of internal motions and provide insight into the energy landscape of proteins. The real challenge, however, is to relate large collective motions to functional properties, such as binding and regulation, or to folding. These issues have been recently addressed in several papers.
Berendsen
H J
HJ
Department of Chemistry, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), The University of Groningen, Groningen, 9747 AG, The Netherlands. berendsen@chem.rug.nl
Hayward
S
S
D000494:Allosteric Regulation; D000818:Animals; D019295:Computational Biology; D003198:Computer Simulation; D003285:Contractile Proteins / Q000737:chemistry; D006801:Humans; D008956:Models, Chemical; D008958:Models, Molecular; D009038:Motion; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D013329:Structure-Activity Relationship
D003285:Contractile Proteins; D011506:Proteins