Ligand-macromolecule interactions are of fundamental importance in the control of biological processes. This book applies the principles of linkage thermodynamics to polyfunctional macromolecular systems under equilibrium conditions, and describes the binding, linkage, and feedback phenomena that lead to control of complex metabolic processes. The first chapter sets out the different processes (conformational changes, changes in state of aggregation, phase changes) involving biological macromolecules which are affected by chemical variables (such as ligands) or physical variables (such as temperature and pressure). The general effects of ligands on micromolecular conformations and interactions are illustrated with specific examples from the respiratory proteins, electron-transport proteins, and nucleic acid binding proteins. Subsequent chapters develop these themes, and describe in detail how the mathematics of regulation and control can be applied to macromolecules in biological system.

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This volume commemorates the 50th anniversary of the appearance in Volume 4 in 1948 of Dr. Jeffries Wyman's famous paper in which he "laid down" the foundations of linkage thermodynamics. Experts in this area contribute articles on the state-of-the-art of this important field and on new developments of the original theory. Among the topics covered in this volume are electrostatic contributions to molecular free energies in solution; site-specific analysis of mutational effects in proteins; allosteric transitions of the acetylcholine receptor; and deciphering the molecular code of hemoglobin allostery.

Essential publication for researchers in all fields of life sciences. Key Features * Major topics covered include: * Deciphering rules of helix stability in peptides * Protein Folding in Membranes * Molecular Crowding * Study of the Bohr Effect in Hemoglobin Intermediates * Photoacoustic Calorimetry of Proteins * Theoretical Aspects of Isothermal Titration Calorimetry * Energetic Methods to Study Bifunctional Biotin Repressor.

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

Ligand binding by macromolecules represents a core event of broad relevance to a range of systems, including catalytic systems alongside noncatalytic systems such as nucleic acid binding by transcription factors or extracellular ligand binding by proteins involved in signaling pathways. The scope of this primer is constrained to introduce only foundational models without significant discussion of more advanced topics such as allosteric or linkage effects. Linkage occurs when the binding of a ligand is influenced by the binding of another molecule of the same ligand (homotropic linkage), the binding of a different ligand (heterotropic linkage), physical variables such as temperature or pressure (physical linkage), or changes in macromolecular assembly state (polysteric linkage). Taking this into account, the foundational themes presented in this primer can be used to describe any macromolecule–ligand interaction either by direct use of the models and techniques described here or by applying them to develop more advanced models to explain additional complexities such as those allosteric or linkage effects just mentioned. The target audience of this primer is the senior undergraduate or junior graduate student who lacks a foundation in ligand-binding thermodynamics. As such, we have focused primarily on foundational thermodynamic treatments and presented only general discussions of relevant experimental designs. Readers of this primer will learn how to build a working understanding of common factors that promote energetic favorability for ligand binding; develop a functional toolbox to understand ligand binding from the perspective of collecting, plotting, and interpreting ligand-binding data; enhance proficiency in deriving thermodynamic mechanisms for ligand binding; and become comfortable in interpreting binding data reported in the literature and independently expanding knowledge beyond the scope introduced in this primer.