Introduction to Macromolecular Binding Equilibria

This compact, graduate-level text focuses on a key area of biophysical chemistry. Introduction to Macromolecular Binding Equilibria first describes the features of binding sites for small molecules and then presents a discussion of the formulation of binding isotherms for simple mathematical models. The book addresses special problems in describing isotherms for linear polymers and examines the complications of binding cooperativity and thermodynamic linkage interactions among multiple ligands. It highlights important aspects of experimental designs, key aspects of ligand binding to planar arrays of sites, and methods for model-free analysis data used to reveal the binding isotherm.

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.

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