title: Global dynamics of proteins: bridging between structure and function.
abstract: Biomolecular systems possess unique, structure-encoded dynamic properties that underlie their biological functions. Recent studies indicate that these dynamic properties are determined to a large extent by the topology of native contacts. In recent years, elastic network models used in conjunction with normal mode analyses have proven to be useful for elucidating the collective dynamics intrinsically accessible under native state conditions, including in particular the global modes of motions that are robustly defined by the overall architecture. With increasing availability of structural data for well-studied proteins in different forms (liganded, complexed, or free), there is increasing evidence in support of the correspondence between functional changes in structures observed in experiments and the global motions predicted by these coarse-grained analyses. These observed correlations suggest that computational methods may be advantageously employed for assessing functional changes in structure and allosteric mechanisms intrinsically favored by the native fold.
authors.affiliation: Department of Computational Biology, School of Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania 15213, USA. bahar@pitt.edu
authors.forename: Ivet
authors.initials: I
authors.lastname: Bahar
authors.forename: Timothy R
authors.initials: TR
authors.lastname: Lezon
authors.forename: Lee-Wei
authors.initials: LW
authors.lastname: Yang
authors.forename: Eran
authors.initials: E
authors.lastname: Eyal
mesh_terms: D008954:Models, Biological; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D013329:Structure-Activity Relationship
chemical_list: D011506:Proteins