title: The role of configurational entropy in biochemical cooperativity.
abstract: Cooperativity is a common biochemical phenomenon in which two or more otherwise independent processes are thermodynamically coupled. Because cooperative processes are usually attended by changes in molecular conformation, thermodynamic coupling is usually attributed to an enthalpy-driven mechanism. In the family of glycopeptide antibiotics that includes vancomycin, however, cooperative phenomena occur that cannot be explained by conformational change. In this communication, we demonstrate that cooperativity in these systems can arise solely from changes in vibrational activity.
authors.affiliation: Department of Pharmacology, University of Pennsylvania, School of Medicine, Philadelphia, Pennsylvania 19104-6084, USA.
authors.forename: Sutjano
authors.initials: S
authors.lastname: Jusuf
authors.forename: Patrick J
authors.initials: PJ
authors.lastname: Loll
authors.forename: Paul H
authors.initials: PH
authors.lastname: Axelsen
mesh_terms: D000409:Alanine / Q000031:analogs & derivatives / Q000737:chemistry / Q000378:metabolism; D000900:Anti-Bacterial Agents / Q000737:chemistry* / Q000378:metabolism; D003198:Computer Simulation; D019281:Dimerization; D008024:Ligands; D008968:Molecular Conformation; D013816:Thermodynamics; D014640:Vancomycin / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism
chemical_list: D000900:Anti-Bacterial Agents; D008024:Ligands; C112142:chloroeremomycin; D014640:Vancomycin; D000409:Alanine