This volume commemorates the 50th anniversary of the appearance in Volume 4 in 1948 of Dr. Jeffries Wyman's famous paper in which he "laid down" the foundations of linkage thermodynamics. Experts in this area contribute articles on the state-of-the-art of this important field and on new developments of the original theory. Among the topics covered in this volume are electrostatic contributions to molecular free energies in solution; site-specific analysis of mutational effects in proteins; allosteric transitions of the acetylcholine receptor; and deciphering the molecular code of hemoglobin allostery.

Proteases occur naturally in all organisms. They are enzymes that are involved in many physiological reactions such as digestion of food and blood clotting. This volume reviews their role in health and disease and presents the latest research and developments.

* Discusses new discoveries, approaches, and ideas * Contributions from leading scholars and industry experts * Reference guide for researchers involved in molecular biology and related fields

This book provides the first systematic treatment of the thermodynamic theory of site-specific effects in biological macromolecules. It describes the phenomenological and conceptual bases required to allow a mechanistic understanding of these effects from analysis of experimental data. The thermodynamic theory also results in novel experimental strategies that enable the derivation of information on local, site-specific properties of a macromolecular system from analysis of perturbed global properties. The treatment focuses on binding phenomena, but is amenable to extension both conceptually and formally to the analysis of other cooperative processes, such as folding and helix coil transitions. This book will interest any scientist involved in structure function studies of biological macromolecules, or as a text for graduate students in biochemistry and biophysics.