Macromolecules in the body form noncovalent associations, such as DNA-protein or protein-protein complexes, that control and regulate numerous cellular functions. Understanding how changes in the concentration and conformation of these macromolecules can trigger physiological responses is essential for researchers developing drug therapies to treat diseases affected by these imbalances.
Introduction to Macromolecular Binding Equilibria gives students in medicinal chemistry, pharmaceuticals, and bioengineering the necessary background in biophysical chemistry for research applications in drug discovery and development. Building upon a fundamental knowledge of calculus and physical chemistry, this compact, graduate-level text prepares students for advanced work in solution thermodynamics and binding phenomena and applying methods in this book to their own research.
This book describes the underlying theory of binding phenomena and explains how to apply the binding polynomial approach for building models and interpreting data. It also covers practical considerations for setting up binding experiments and describes how to obtain true thermodynamic isotherms unbiased by model assumption via model-free analysis of binding data.
Binding sites. Binding isotherms. Binding linkage, binding competition, and multiple ligand species. Cooperativity. Binding to lattices of sites. Choosing a method and analyzing the data. Appendix: The sequence-generating function method. Index