title: The energy landscapes and motions of proteins.
abstract: Recent experiments, advances in theory, and analogies to other complex systems such as glasses and spin glasses yield insight into protein dynamics. The basis of the understanding is the observation that the energy landscape is complex: Proteins can assume a large number of nearly isoenergetic conformations (conformational substates). The concepts that emerge from studies of the conformational substates and the motions between them permit a quantitative discussion of one simple reaction, the binding of small ligands such as carbon monoxide to myoglobin.
authors.affiliation: Center for Advanced Study, University of Illinois, Champaign, Urbana 61801.
authors.forename: H
authors.initials: H
authors.lastname: Frauenfelder
authors.forename: S G
authors.initials: SG
authors.lastname: Sligar
authors.forename: P G
authors.initials: PG
authors.lastname: Wolynes
mesh_terms: D002248:Carbon Monoxide / Q000737:chemistry; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D009038:Motion; D009211:Myoglobin / Q000737:chemistry*; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D013696:Temperature; D013816:Thermodynamics
chemical_list: D009211:Myoglobin; D002248:Carbon Monoxide