Linkage Thermodynamics of Macromolecular InteractionsEdited by
- Enrico Di Cera
- Frederic Richards
- David Eisenberg
- Peter Kim
Biochemists, molecular biologists, biophysicists, and biomedical researchers.
Advances in Protein Chemistry and Structural Biology
Hardbound, 473 Pages
Published: May 1998
Imprint: Academic Press
"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...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... This volume is highly recommended for protein chemists, molecular or cell biologists who need a better understanding of these topics."
Praise for the Volume, --DOODY'S PUBLISHING REVIEWS (4 star rating)
"The authority, originality, and editing of the reviews are first class."
Praise for the Series, --NATURE
"The Advances in Protein Chemistry series has been a major factor in the education of protein chemists."
--JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- M. Schaefer, H. van Vlijmen, and M. Karplus, Electrostatic Contributions to Molecular Free Energies in Solution.E. Di Cera, Site-Specific Analysis of Mutational Effects in Proteins.S.J. Edelstein and J.-P. Changeux, Allosteric Transitions of the Acetylcholine Receptor.G.K. Ackers, Deciphering the Molecular Code of Hemoglobin Allostery.E. Freire, Statistical Thermodynamic Linkage between Conformational and Binding Equilibria.M.T. Record, Jr., W. Zhang, and C.F. Anderson, Analysis of the Effects of Salts and Uncharged Solutes on Protein and Nucleic Acid Equilibria and Processes: A Practical Guide to Recognizing and Interpreting Polyelectrolyte Effects, Hofmeister Effects, and Osmotic Effects of Salts.S.N. Timasheff, Control of Protein Stability and Reactions by Weakly Interacting Cosolvents: The Simplicity of the Complicated.Author Index.Subject Index.