This book presents a detailed examination of the physical properties of proteins and their associations with solvents, ligands, and each other. Incorporating observations from his classic work on the thermodynamics of protein-protein and protein-ligand interactions, the internationally recognized author offers a complete conceptual and quantitative description of proteins and their associations. The book begins with an overview of basic thermodynamic principles and goes on to describe the covalent and noncovalent binding of single and multiple ligands and their effects on protein-protein associations. Discussions of protein-solvent interactions address issues including protein folding, membrane associations, and protein dynamics. Attention is given to the effect of temperature and pressure on protein structure, oligomerization, and ligand binding, as well as to ideas about the basis of biological specificity. Although experimental work is discussed throughout the text, the book is not technique oriented. Its theoretical framework is clear, general and easily understandable, making this an essential textbook for beginning graduate students in biological sciences, as well as a valuable reference for advanced researchers in industry and academia.
`The majority of the material in the book comes from observations made by Weber himself, work that has won him numerous awards and international recognition...The theoretical framework is elementary enough to be appreciated by beginning graduate students in the biological sciences: this would make an excellent textbook for advanced courses. ...the reader is bound to come away with a better understanding of protein systems. I highly recommend this book to all who study proteins.'
The Quarterly Review of Biology
`Many people will enjoy reading this book... As for recommending it to graduate students, I would only give it to critical ones with high grades. It will sharpen their wits!'
`Weber's book is accessible, well written, and of high quality.... should be in the personal libraries of all serious physical biochemists and should be made available as supplementary texts and references for students in graduate physical biochmistry and advanced biochemistry courses.'
Trends in Biochemical Sciences
Thermodynamic fundamentals; The chemical potentials of proteins; Simultaneous ligand-protein equilibria; Binding of the same ligand at multiple protein sites: Adair formulation; Multiple binding with ligand interactions; Ligand distribution and binding asymmetry; Binding by multiple proteins; Hemoglobin I; Hemoglobin II; Equilibria involving covalent and non-covalent ligands; Intramolecular and solvent interactions of proteins; Transfer of proteins between phases: the dynamic interactions of proteins with membranes; Detection and measurement of the statics and dynamics of protein-ligand and protein-protein interactions; Effects of temperature and pressure upon molecular associations and upon single chain proteins; Dissociation of protein dimers; Effect of pressure upon oligomeric proteins and protein aggregates; Biological specificity and ligand binding.