Reversible ligand binding: theory and experiment

Reversible Ligand Binding: Theory and Experiment discusses the physical background of protein-ligand interactions—providing a comprehensive view of the laws that govern reversible, as well as irreversible, ligand binding. Special consideration is devoted to enzymology, a field usually treated separately from ligand binding, but actually governed by identical thermodynamic relationships. Attention is given to the design of experiments, including how to uncover evidence of biochemical features that may otherwise escape notice. Classical experiments are reviewed in order to further highlight the importance of the experimental design. Overall, the book supplies students with understandingnecessary for interpreting ligand binding experiments, formulating plausible reaction schemes, and analyzing the data according to a chosen model. Topics covered include: theory of ligand binding to monomeric proteins; practical considerations and commonly encountered problems; oligomeric proteins with multiple binding sites; ligand binding kinetics; hemoglobin and its ligands; single-substrate enzymes and their inhibitors; two-substrate enzymes and their inhibitors; and rapid kinetic methods for studying enzyme reactions.