title: How to Distinguish Conformational Selection and Induced Fit Based on Chemical Relaxation Rates.
abstract: Protein binding often involves conformational changes. Important questions are whether a conformational change occurs prior to a binding event ('conformational selection') or after a binding event ('induced fit'), and how conformational transition rates can be obtained from experiments. In this article, we present general results for the chemical relaxation rates of conformational-selection and induced-fit binding processes that hold for all concentrations of proteins and ligands and, thus, go beyond the standard pseudo-first-order approximation of large ligand concentration. These results allow to distinguish conformational-selection from induced-fit processes-also in cases in which such a distinction is not possible under pseudo-first-order conditions-and to extract conformational transition rates of proteins from chemical relaxation data.
authors.affiliation: Max Planck Institute of Colloids and Interfaces, Department of Theory and Bio-Systems, Potsdam, Germany.|Free University Berlin, Department of Mathematics and Computer Science, Berlin, Germany.
authors.forename: Fabian
authors.identifier: 0000-0002-1478-1827
authors.initials: F
authors.lastname: Paul
authors.affiliation: Max Planck Institute of Colloids and Interfaces, Department of Theory and Bio-Systems, Potsdam, Germany.
authors.forename: Thomas R
authors.identifier: 0000-0002-0911-5328
authors.initials: TR
authors.lastname: Weikl
mesh_terms: D019295:Computational Biology; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins