title: Intrinsic dynamics of enzymes in the unbound state and relation to allosteric regulation.
abstract: In recent years, there has been a surge in the number of studies exploring the relationship between proteins' equilibrium dynamics and structural changes involved in function. An emerging concept, supported by both theory and experiments, is that under native state conditions proteins have an intrinsic ability to sample conformations that meet functional requirements. A typical example is the ability of enzymes to sample open and closed forms, irrespective of substrate, succeeded by the stabilization of one form (usually closed) upon substrate binding. This ability is structure-encoded, and plays a key role in facilitating allosteric regulation, which suggests complementing the sequence-encodes-structure paradigm of protein science by structure-encodes-dynamics-encodes-function. The emerging connection implies an evolutionary role in selecting/conserving structures based on their ability to achieve functional dynamics, and in turn, selecting sequences that fold into such 'apt' structures.
authors.affiliation: Department of Computational Biology, School of Medicine, University of Pittsburgh, Suite 3064, Biomedical Science Tower 3, 3051 Fifth Avenue, Pittsburgh, PA 15213, USA. bahar@pitt.edu
authors.forename: Ivet
authors.initials: I
authors.lastname: Bahar
authors.forename: Chakra
authors.initials: C
authors.lastname: Chennubhotla
authors.forename: Dror
authors.initials: D
authors.lastname: Tobi
mesh_terms: D000494:Allosteric Regulation; D004798:Enzymes / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D011487:Protein Conformation
chemical_list: D004798:Enzymes