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

Multiple Equilibria in Proteins covers the multiple interactions between small ions and molecules and a protein molecule. The book also deals with the physicochemical mechanisms of this interaction and the information about protein structure and the forces stabilizing that structure. The text discusses the mathematical description of complex formation, the thermodynamic analysis of binding data, and various theoretical models which can be used to describe the phenomena of small molecule-macromolecule interactions. The measurement of complex formation; the binding of neutral molecules; and hydrogen-ion equilibria are also considered. The book further tackles metal-ion binding; the binding of organic ions by proteins; as well as protein-protein interaction. Chemists and biochemists will find the book useful.

This book presents a unified description of binding equilibrium for a wide variety of systems focusing on acid-base and coordination chemistry, adsorption at interfaces, and electron binding in electrochemistry. It overviews more complex phenomena such as competitive binding to different sites and of different ligands. Multiple sites such as those occurring in macromolecules, colloidal oxides, humid substances, and proteins are briefly discussed and many experimental results for these types of systems are analyzed. Titrations and consideration of the distribution of binding constants are also presented. The book is mainly directed at undergraduate/graduate students of chemistry, biology, and earth sciences. It is supplementary to the standard physical and analytical chemistry courses and will help both students and teachers get a more in-depth knowledge and understanding of the systems analyzed.

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.

Progressively builds a deep understanding of macromolecular behavior Based on each of the authors' roughly forty years of biophysics research and teaching experience, this text instills readers with a deep understanding of the biophysics of macromolecules. It sets a solid foundation in the basics by beginning with core physical concepts such as thermodynamics, quantum chemical models, molecular structure and interactions, and water and the hydrophobic effect. Next, the book examines statistical mechanics, protein-ligand binding, and conformational stability. Finally, the authors address kinetics and equilibria, exploring underlying theory, protein folding, and stochastic models. With its strong emphasis on molecular interactions, Equilibria and Kinetics of Biological Macromolecules offers new insights and perspectives on proteins and other macromolecules. The text features coverage of: Basic theory, applications, and new research findings Related topics in thermodynamics, quantum mechanics, statistical mechanics, and molecular simulations Principles and applications of molecular simulations in a dedicated chapter and interspersed throughout the text Macromolecular binding equilibria from the perspective of statistical mechanics Stochastic processes related to macromolecules Suggested readings at the end of each chapter include original research papers, reviews and monographs, enabling readers to explore individual topics in greater depth. At the end of the text, ten appendices offer refreshers on mathematical treatments, including probability, computational methods, Poisson equations, and defining molecular boundaries. With its classroom-tested pedagogical approach, Equilibria and Kinetics of Biological Macromolecules is recommended as a graduate-level textbook for biophysics courses and as a reference for researchers who want to strengthen their understanding of macromolecular behavior.

This comprehensive text offers a solid introduction to the biochemical principles and skills required for any researcher applying computational tools to practical problems in biochemistry. Each chapter includes an introduction to the topic, a review of the biological concepts involved, a discussion of the programming and applications used, key references, and problem sets and answers. Providing detailed coverage of biochemical structures, enzyme reactions, metabolic simulation, genomic and proteomic analyses, and molecular modeling, this is the perfect resource for students and researchers in biochemistry, bioinformatics, bioengineering and computational science.

Fully updated and expanded-a solid foundation for understandingexperimental enzymology. This practical, up-to-date survey is designed for a broadspectrum of biological and chemical scientists who are beginning todelve into modern enzymology. Enzymes, Second Editionexplains the structural complexities of proteins and enzymes andthe mechanisms by which enzymes perform their catalytic functions.The book provides illustrative examples from the contemporaryliterature to guide the reader through concepts and data analysisprocedures. Clear, well-written descriptions simplify the complexmathematical treatment of enzyme kinetic data, and numerouscitations at the end of each chapter enable the reader to accessthe primary literature and more in-depth treatments of specifictopics. This Second Edition of Enzymes: A Practical Introductionto Structure, Mechanism, and Data Analysis features refinedand expanded coverage of many concepts, while retaining theintroductory nature of the book. Important new featuresinclude: A new chapter on protein-ligand binding equilibria Expanded coverage of chemical mechanisms in enzyme catalysisand experimental measurements of enzyme activity Updated and refined discussions of enzyme inhibitors andmultiple substrate reactions Coverage of current practical applications to the study ofenzymology Supplemented with appendices providing contact information forsuppliers of reagents and equipment for enzyme studies, as well asa survey of useful Internet sites and computer software forenzymatic data analysis, Enzymes, Second Edition isthe ultimate practical guide for scientists and students inbiochemical, pharmaceutical, biotechnical, medicinal, andagricultural/food-related research.