Physical Principles And Techniques Of Protein Chemistry Part C

Physical Principles and Techniques of Protein Chemistry, Part C focuses on the effects of intermolecular interactions that are transmitted between ligands and proteins and from protein to protein. This book discusses the density and volume change measurements; direct volume change; osmotic pressure; and small-angle X-ray scattering. The theory of particulate scattering; pulsed nuclear magnetic resonance; absorption of water by diamagnetic molecules; and use of least squares in data analysis are also elaborated. This text likewise covers the iteration process; optical rotatory dispersion and the main chain conformation of proteins; and basic relations for optically active molecules. Other topics include the circular dichroism, secondary structure of proteins, visible rotatory dispersion, and peptide cotton effects. This publication is intended for protein chemists, but is also useful to biologists, medical practitioners, and students researching on protein chemistry.

Physical Principles and Techniques of Protein Chemistry, Part B deals with the theories and application of selected physical methods in protein chemistry evaluation. This book is divided into seven chapters that cover the ultracentrifugal analysis, light scattering, infrared (IR) methods, nuclear magnetic resonance (NMR) spectroscopy, and differential thermal analysis of protein properties. This text first describes the fundamental ideas and methodology of sedimentation analysis of ideal noninteracting solutes and the problems of nonideality and solute-solute interaction. This book then deals with the problems involved in the interpretation of viscometric data for evaluation of intrinsic viscosity of proteins. The following chapters examine the principles, measurement and analysis of spectra, and experimental techniques of light scattering, IR, and NMR spectroscopic methods. Discussions on coordination phenomena, identification of binding sites, and ion binding in the crystalline state and in protein solutions are included. The concluding chapter presents some examples of protein analysis using differential thermal analysis technique. This book is of great value to chemists, biologists, and researchers who have great appreciation of protein chemistry.

Physical Principles and Techniques of Protein Chemistry, Part A deals with the principles and application of selected physical methods in protein chemistry evaluation. This book is organized into nine chapters that cover microscopic, crystallographic, and electrophoretic techniques for protein conformational perturbations evaluation. This text first presents a general account of electron microscopy, its specimen preparation, optimum conditions for high resolution, measurement of electron micrographs, and illustrative examples of protein study. This book then examines the different types of maps from X-ray methods and the diffraction data from fibrous proteins. The subsequent chapters cover discussions on UV spectroscopy of proteins; luminescence properties of proteins and related compounds; and perturbation and flow methods for evaluation of proteins’ dynamic properties and rate constants. Other chapters deal with the evaluation of proteins’ dielectric properties using dielectric relaxation, electric birefringence, and dichroism techniques. The concluding chapters outline the theoretical and experimental advances of the electrophoretic and gel filtration methods for the study of protein structure and molecular weight. This book is of great value to chemists, biologists, and researchers who have great appreciation of protein chemistry.

This book has been written in part with the aim of providing a text which will be useful in teaching the biochemical applications of spectroscopy. This book will be of particular use to the biochemist or biologist who does not have a background in spectroscopy, but desires to find out what sort of information spectroscopy can provide. Attention was limited to those techniques most frequently used, and which at present have the widest applications.

Amino acids are featured in course syllabuses and in project and research work over a wide spectrum of subject areas in chemistry and biology. Chemists and biochemists using amino acids have many common needs when they turn to the literature for comprehensive information. Among these common interests, analytical studies, in particular, have undergone rapid development in recent years. All other chemical and biochemical aspects of amino acids - synthesis, properties and reactions, preparation of derivatives for use in peptide synthesis, racemization and other fundamental mechanistic knowledge - have been the subject of vigorous progress. This book offers a thorough treatment of all these developing areas, and is structured in the belief that biochemists, physiologists and others will profit from access to information on topics such as the physical chemistry of amino acid solutions, as well as from thorough coverage of amino acid metabolism, biosynthesis and enzyme inhibition; and that chemists will find relevant material in biological areas as well as in the analysis, synthesis and reactions of amino acids.