title: Kinetic studies of protein-protein interactions.
abstract: The structure of a protein-protein interaction, its affinity and thermodynamic characteristics depict a 'frozen' state of a complex. This picture ignores the kinetic nature of complex formation and dissociation, which are of major biological and biophysical interest. This review highlights recent advances in deciphering the kinetic pathway of protein-protein complexation, the nature of the encounter complex, transition state and intermediate along the reaction, and the effects of mutation, viscosity, pH and salt on association.
authors.affiliation: Department of Biological Chemistry, Weizmann Institute of Science, 76100, Rehovot, Israel. bcges@weizmann.ac.il
authors.forename: Gideon
authors.initials: G
authors.lastname: Schreiber
mesh_terms: D000818:Animals; D001665:Binding Sites / Q000502:physiology*; D006801:Humans; D007700:Kinetics; D011485:Protein Binding / Q000502:physiology*; D013816:Thermodynamics