This is the first book that attempts to study the origin of cooperatvity in binding systems from the molecular point of view. The molecular approach provides a deeper insight into the mechanism of cooperativity and regulation, than the traditional phenomenological approach.
This book uses the tools of statistical mechanics to present the molecular theory of cooperativity. Cooperativity is used in a variety of processes-such as loading and unloading of oxygen at relatively small pressure differences; maintaining an almost constant concentration of various compounds in living cells; and switching on and off the reading of genetic information.
This book may be used as a textbook by graduate students in Chemistry, Biochemistry and Biophysics, and will also be of interest to researchers in theoretical biochemistry.
1. Introducing the Fundamental Concept. 2. The Binding Isotherm (BI). 3. Adsorption on a Single Polymer with Conformation Changes Induced by the Binding Process. 4. Two-site Systems; Direct and Indirect Cooperativity. 5. Three-site Systems; Non-additivity and Long Range Correlations. 6.7. Large Linear Systems of Binding Sites. 8. Regulatory Enzymes. 9. Solvent Effects on Cooperativity. 10. Appendices. Appendix A: Pair and triple correlations between events. Appendix B: Localization of the adsorbent molecules, and its effect on the binding isotherm. Appendix C: Transition from microstates to macrostates. Appendix D: First order correction to non-ideality of the ligand's reservoir. Appendix E: Relative slopes of the equilibrated and "frozen in" BI's in a multi macrostate system. Appendix F: Spurious cooperativity in single-site systems. Appendix G: The relation between the binding isotherm and the titration curves for two-site systems. Appendix H: Synthetic data. Appendix I: A comment on nomenclature. Appendix J: Average binding constants and correlation functions. Appendix K: Utility function in binding systems.