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.

This volume successfully and clearly examines how biophysical approaches can be used to study complex systems of reversibly interacting proteins. It deals with the methodology behind the research and shows how to synergistically incorporate several methodologies for use. Each chapter treats and introduces the reader to different biological systems, includes a brief summary of the physical principles, and mentions practical requirements.

Reductionism as a scientific methodology has been extraordinarily successful in biology. However, recent developments in molecular biology have shown that reductionism is seriously inadequate in dealing with the mind-boggling complexity of integrated biological systems. This title presents an appropriate balance between science and philosophy and covers traditional philosophical treatments of reductionism as well as the benefits and shortcomings of reductionism in particular areas of science. Discussing the issue of reductionism in the practice of medicine it takes into account the holistic and integrative aspects that require the context of the patient in his biological and psychological entirety. The emerging picture is that what first seems like hopeless disagreements turn out to be differences in emphasis. Although genes play an important role in biology, the focus on genetics and genomics has often been misleading. The consensus view leads to pluralism: both reductionst methods and a more integrative approach to biological complexity are required, depending on the questions that are asked. * An even balance of contributions from scientists and philosophers of science - representing a unique interchange between both communities interested in reductionism

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.

A reissue of a classic book -- corrected, edited, typeset, redrawn, and indexed for the Biological Physics Series. Intended for undergraduate courses in biophysics, biological physics, physiology, medical physics, and biomedical engineering, this is an introduction to statistical physics with examples and problems from the medical and biological sciences. Topics include the elements of the theory of probability, Poisson statistics, thermal equilibrium, entropy and free energy, and the second law of thermodynamics. It can be used as a supplement to standard introductory physics courses, and as a text for medical schools, medical physics courses, and biology departments. The three volumes combined present all the major topics in physics. These books are being reissued in response to frequent requests to satisfy the growing need among students and practitioners in the medical and biological sciences with a working knowledge of the physical sciences. The books are also in demand in physics departments either as supplements to traditional intro texts or as a main text for those departments offering courses with biological or medical physics orientation.

The aim of the book is to introduce the reader to the kinetic analysis of a wide range of biological processes at the molecular level. It is intended to show that the same approach can be used to resolve the number of steps in enzyme reactions, muscle contraction, visual perception and ligand binding receptors that trigger other physiological processes. Attention is also given to methods for characterizing these steps in chemical terms. Although the treatment is mainly theoretical, a wide range of examples and experimental techniques are also introduced and an historical approach is used to demonstrate the development of the theory and experimental techniques of kinetic analysis in biology.

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.

Explores new applications emerging from our latest understanding of proteins in solution and at interfaces Proteins in solution and at interfaces increasingly serve as the starting point for exciting new applications, from biomimetic materials to nanoparticle patterning. This book surveys the state of the science in the field, offering investigators a current understanding of the characteristics of proteins in solution and at interfaces as well as the techniques used to study these characteristics. Moreover, the authors explore many of the new and emerging applications that have resulted from the most recent studies. Topics include protein and protein aggregate structure; computational and experimental techniques to study protein structure, aggregation, and adsorption; proteins in non-standard conditions; and applications in biotechnology. Proteins in Solution and at Interfaces is divided into two parts: Part One introduces concepts as well as theoretical and experimental techniques that are used to study protein systems, including X-ray crystallography, nuclear magnetic resonance, small angle scattering, and spectroscopic methods Part Two examines current and emerging applications, including nanomaterials, natural fibrous proteins, and biomolecular thermodynamics The book's twenty-three chapters have been contributed by leading experts in the field. These contributions are based on a thorough review of the latest peer-reviewed findings as well as the authors' own research experience. Chapters begin with a discussion of core concepts and then gradually build in complexity, concluding with a forecast of future developments. Readers will not only gain a current understanding of proteins in solution and at interfaces, but also will discover how theoretical and technical developments in the field can be translated into new applications in material design, genetic engineering, personalized medicine, drug delivery, biosensors, and biotechnology.

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

This comprehensive book presents a modern concept in biophysics based on recently published research. It highlights various aspects of the biophysical fundamentals and techniques that are currently used to study different physical properties of biomolecules, and relates the biological phenomenon with the underlying physical concepts. The content is divided into nine chapters summarizing the structural details of proteins, including recently discovered novel folds, higher order structures of nucleic acids, as well as lipids and the physical forces governing the macromolecular interactions which are essential for the various biological processes. It also provides insights into the recent advances in biophysical techniques including Hydrogen Deuterium Exchange with Mass Spectrometry (HDX-MS), Small angle X-ray scattering (SAXS) and Cryo Electron Microscopy (cryo EM), supplemented with interesting experimental data. It is a valuable reference resource for anyone with a desire to gain a better understanding of the fundamentals of biophysical concepts and techniques of important biomolecules.