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From The CriticsReviewer: Gene A. Homandberg, PhD (Rush Medical College of Rush University)
Description: This Advances in Protein Chemistry volume on linkage thermodynamics of macromolecular interactions introduces and updates topics dealing with the role of electrostatic contributions to free energies of soluble molecules, analysis of mutational effects on protein interactions, allosteric transitions of acetylcholine receptor, hemoglobin allostery, statistical thermodynamic linkage between conformations and binding equilibria, effects of salts and solutes on protein and nucleic acid equilibria, and effect of cosolvents on protein stability and reactions.
Purpose: It is meant to present selected topics on the role of linkage thermodynamics in explaining protein folding, protein stability, allostery, and protein-ligand interaction. The contributions are by outstanding investigators who bring both a traditional perspective on this topic and expertise and knowledge in newer aspects and applications, such as protein-nucleic acid interactions.
Audience: The material is aimed at the specialist, but an introduction or overview for the less initiated would have been helpful. Nonetheless, any investigator with interests in protein folding and stability, or protein-protein or protein-ligand interaction thermodynamics or in enzyme or receptor interaction thermodynamics should find this volume useful and informative.
Features: This attractive volume is of the quality of all of the books in the series and has the typical high quality text, figures, and subject index.
Assessment: This volume is highly recommended for protein chemists, molecular or cell biologists who need a better understanding of these topics. With such a detailed overview of these specific concepts, there is something in these chapters for everyone.