On the day after the 1959 Cambridge Congress, during which the International Union of Pure and Applied Biophysics was founded, a biophysics section was formed within the Society of Physical Chemistry (Societe de Chimie Physique). Since then, three of the Society's annual meetings (the 11th, 17th, and 23rd) were devoted exclusively to the physico-chemical study of biological systems. The first of these was held in June 1961 at a hotel in Col de Voza, at the foot of an alpine glacier above Chamonix. The second, in May 1967, took place in the more learned setting of the venerable rooms of the National Museum of Natural History in Paris. The third - the one dealt with in the present volume - was recently held at Orleans-La Source in the newly built lecture theatres of the young University, which is near the great Institutes of the National Centre for Scientific Research (CNRS), on the Sologne plateau. These three stages are milestones of an evolution which characterises (at least schematically) the explosive evolution of biological physico-chemistry. The first colloquium, with the title 'Deoxyribonucleic Acid: Structure, Synthesis and Functions', actually marks the first contact of the physical chemist with one of the then most prestigious biological macromolecules, the structure of which had just been discovered, and in this way celebrated one of the first and most striking successes of molecular biology.

This book discusses how biological molecules exert their function and regulate biological processes, with a clear focus on how conformational dynamics of proteins are critical in this respect. In the last decade, the advancements in computational biology, nuclear magnetic resonance including paramagnetic relaxation enhancement, and fluorescence-based ensemble/single-molecule techniques have shown that biological molecules (proteins, DNAs and RNAs) fluctuate under equilibrium conditions. The conformational and energetic spaces that these fluctuations explore likely contain active conformations that are critical for their function. More interestingly, these fluctuations can respond actively to external cues, which introduces layers of tight regulation on the biological processes that they dictate. A growing number of studies have suggested that conformational dynamics of proteins govern their role in regulating biological functions, examples of this regulation can be found in signal transduction, molecular recognition, apoptosis, protein / ion / other molecules translocation and gene expression. On the experimental side, the technical advances have offered deep insights into the conformational motions of a number of proteins. These studies greatly enrich our knowledge of the interplay between structure and function. On the theoretical side, novel approaches and detailed computational simulations have provided powerful tools in the study of enzyme catalysis, protein / drug design, protein / ion / other molecule translocation and protein folding/aggregation, to name but a few. This work contains detailed information, not only on the conformational motions of biological systems, but also on the potential governing forces of conformational dynamics (transient interactions, chemical and physical origins, thermodynamic properties). New developments in computational simulations will greatly enhance our understanding of how these molecules function in various biological events.

Proceedings of a Colloquium held at Orléans, France, July 5-9, 1982

First multi-year cumulation covers six years: 1965-70.

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.