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 thesis addresses optical binding - a new area of interest within the field of optical micromanipulation. It presents, for the first time, a rigorous numerical simulation of some of the key results, along with new experimental findings and also physical interpretations of the results. In an optical trap particles are attracted close to areas of high optical intensities and intensity gradients. So, for example, if two lasers are pointed towards each other (a counter propagating trap) then a single particle is trapped in the centre of the two beams – the system is analogous to a particle being held by two springs in a potential well. If one increases the number of particles in the trap then naively one would expect all the particles to collect in the centre of the well. However, the effect of optical binding means that the presence of one particle affects the distribution of light experienced by another particle, resulting in extremely complex interactions that can lead to unusual 1D and 2D structures to form within the trap. Optical binding is not only of theoretical interest but also has applications in micromanipulation and assembly.

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.

Cell Surface Receptors: A Short Course on Theory and Methods, 3rd Edition, links theoretical insights into drug-receptor interactions described in mathematical models with the experimental strategies to characterize the biological receptor of interest. The study of receptors has changed considerably over the period of the publication of the three editions of this book. The cloning of several genomes makes it unlikely that preparations of receptors now or in the future will arise from their purification as trace proteins from native tissues, but rather from a myriad of molecular approaches. Nonetheless, understanding the molecular mechanisms and ultimately the in vivo biology of these receptors means that investigators will engage in molecular, cellular and ultimate in vivo strategies. It should be of value to investigators who want to identify, characterize and understand the biology of a receptor of interest.

A Pharmacology Primer: Techniques for More Effective and Strategic Drug Discovery, Fifth Edition features the latest ideas and research regarding the application of pharmacology to the process of drug discovery. Written by well-respected pharmacologist, Terry P. Kenakin, this primer is an indispensable resource for all those involved in drug discovery. This updated edition has been thoroughly revised to include material on quantifying drug efficacy through bias and cluster analysis, the impact of molecular dynamics and protein structural analysis, the real time kinetic analysis of drug effect, virtual screening for new drug chemical scaffolds, and much more. With full color illustrations and new examples throughout, this book remains a top reference for all industry and academic scientists that is also ideal for students directly involved in drug discovery or pharmacologic research. - Highlights changes surrounding strategies for drug discovery, providing a comprehensive reference and featuring advances in the methods involved - Includes multiple new sections, such as development and utilization of models in pharmacology, de-orphanization of new drug targets, predicting impact of disease on drug pharmacokinetics, and the impact of enzyme kinetics on drug-drug interactions - Illustrates the application of rapid inexpensive assays to predict activity in the therapeutic setting, showing data outcomes and the limitations inherent in interpreting this data

This guide has been designed especially for scientists trained in molecular biology and related fields who now need to know more about the basic theories, principles and practical applications of pharmacology.

This text traces developments in rational drug discovery and combinatorial library design with contributions from 50 leading scientists in academia and industry who offer coverage of basic principles, design strategies, methodologies, software tools and algorithms, and applications. It outlines the fundamentals of pharmacophore modelling and 3D Quantitative Structure-Activity Relationships (QSAR), classical QSAR, and target protein structure-based design methods.