Organized into five chapters, this volume starts with an overview of the fluorometric methods for analysis of peptides and proteins with focus on their use in high performance liquid chromatography. This text then presents a thorough discussion on partition chromatography of proteins and peptides. Other chapters consider a comprehensive account of absorption and fluorescence techniques for the structural analysis of proteins. This book presents as well a comprehensive discussion on optical rotatory dispersion and circular dichroism methods and their application for the study of protein conformation. The final chapter deals with the historical aspects of fetuin and ultracentrifuge.
This book is a valuable resource for chemists, biologists, endocrinologists, and physicians.
With its wide range of topics and long historical pedigree, Advances in Enzymology and Related Areas of Molecular Biology can be used not only by students and researchers in molecular biology, biochemistry, and enzymology, but also by any scientist interested in the discovery of an enzyme, its properties, and its applications.
Organized into three parts encompassing 24 chapters, this volume begins with an overview of the structure of polyglycine II with chains running in opposite directions as indicated by the existence of lamellar crystals in electron microscopy. This text then explores the capability of various polypeptides to form the collagen fold. Other chapters consider the effect of pyrrolidine residues on the helix–coil transitions of different native collagens and cross-linked single chain gelatins. This book discusses as well the results of hydrodynamic experiments on native amylose. The final chapter deals with X-ray and electron microscope studies, which are described for two principal types of chitin–protein complex found in insect cuticles.
This book is a valuable resource for physicists, biophysicists, crystallographers, and research workers.
This book outlines first the quantitative procedures and various methods suitable for the determination of amino acids found as constituents of naturally occurring peptides and as free amino acids in tissues and body fluids. These topics are followed by a discussion on some of the aspects of peptide chemistry, which appear significant in relation to peptides possessing physiological activity. The next chapter considers protein synthesis that represents the sequences of chemical reactions whereby amino acids are assembled in biological systems to produce proteins. This volume also examines the correlation of structure with function; the mechanisms of control of protein biosynthesis; the exact role of
intramolecular interactions in the determination of tertiary structure; and the colinearity of genetic “maps with amino acid sequences. A chapter describes the methods of analysis and reactions of sulfhydryl, disulfide, and thiol ester groups in proteins, as well as the evidence relating to the functions of these sulfur groups in proteins. The final chapter looks into the models and theories for the noncovalent bond interactions in proteins.
This book is of value to organic chemists, biochemists, and researchers in the protein-related fields.
The opening chapter presents interpretative procedures of experimental methods for determining protein conformation using X-ray crystallography, followed by an examination of the acid-base dissociations of proteins. The discussion then shifts to the investigation of interactions between protein molecules and other macromolecules, which is of significant importance in providing a chemical basis for many biological processes. A chapter considers first the synthesis, purification, and chemical properties of the polyamino acids. This chapter further describes their physicochemical properties in the solid state, in solution, and at interfaces, and lastly discusses their biological properties as high molecular weight substrates for proteolytic enzymes and as synthetic antigens, and their interaction with proteins and nucleic acids, with viruses, bacteria, blood components, and other biological systems. The use of polyamino acids in the study of the genetic code and the preparation and properties of polypeptidyl proteins are also covered. The concluding chapter focuses on X-ray analysis of protein structure.
Organic chemists, biochemists, and researchers in protein-related fields will find this book invaluable
The publication first elaborates on biochemistry and geochemistry, water and its biological significance, and the problems of protein structure. Discussions focus on the number of peptide chains in the molecule and nature of terminal groups, latent heat of fusion, characteristics of the amino acids derived from proteins, expansion of water in freezing, and the relative abundance of chemical elements in the universe. The text then takes a look at thermodynamics and the application to polar molecules and ionic solutions of electrostatics, including free energy of a charged sphere, image charges, salting-out effect, expressions for the change of fundamental thermodynamic functions, and chemical potentials.
The book examines the conductivity of electrolytes, acid-base equilibria, and polybasic acids, bases, and ampholytes, including proteins. Topics include ionization of cysteine, isoelectric points of polyvalent ampholytes, hemoglobin, nature of acids and bases, measurement of conductivity, electrolytes as conductors, and the moving boundary method of determining transference numbers.
The manuscript is a dependable reference for chemists and researchers interested in thermodynamics, electrostatics, and the biological value of the properties of matter.