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.