Physical Principles and Techniques of Protein Chemistry Part C PDF Download
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Author: Sydney Leach
Publisher: Elsevier
ISBN: 0323141145
Category : Science
Languages : en
Pages : 639
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Book Description
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.
Author: Sydney Leach
Publisher: Elsevier
ISBN: 0323141145
Category : Science
Languages : en
Pages : 639
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Book Description
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.
Author: Sidney Udenfriend
Publisher: Elsevier
ISBN: 1483218007
Category : Science
Languages : en
Pages : 516
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Book Description
The Peptides: Analysis, Synthesis, Biology, Volume 7: Conformation in Biology and Drug Design focuses on the analysis of peptides, emphasizing the use of physical methods in peptide conformational analysis and the relationship of conformational properties of peptides to biological properties. This book consists of nine chapters. Chapter 1 provides a brief overview of the perspective on the application of physical methods to peptide conformational analysis. The use of circular dichroism (CD) spectroscopy to examine the conformational properties of peptides in solution is elaborated in Chapter 2, while the use of fluorescence spectroscopy to examine the special relationships of aromatic side-chain groups to one another is discussed in Chapter 3. In Chapter 4, the use of various theoretical methods to calculate the conformations of peptides is described. The methods used to stimulate peptide conformations and dynamics are outlined in Chapter 5. The last four chapters examine various aspects of the use of nuclear magnetic resonance (NMR) in peptide conformational analysis. This volume is suitable for biologists, specialists, and researchers interested in peptides and proteins.
Author: Herbert Taylor
Publisher: Elsevier
ISBN: 0323151876
Category : Science
Languages : en
Pages : 407
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Book Description
Molecular Genetics, Part III: Chromosome Structure explores the structure and modification of DNA, chromatin, and higher order organization and possible subunits of chromosomes at the molecular level. It describes major changes in concepts of chromatin structure and packaging of DNA based on studies of nuclease digests and electron micrographs; the role of restriction endonucleases in molecular genetics; the involvement of DNA topoisomerases in concerted breaking and rejoining of DNA backbone bonds; enzymatic methylation of DNA; and transcriptional units in eukaryotic chromosomes. Organized into seven chapters, this volume begins with an overview of the general properties of type I and type II restriction enzymes, basic aspects of restriction enzyme technology, and applications of restriction enzyme technology to the study of chromosome structure and function. It then discusses recombinant DNA technology; possible biological roles of DNA topoisomerases; recognition and control sequences in nucleic acids; composition and substructure of nucleosomes; analysis of chromosome fibers by electron microscopy; organization of fibers into chromosomes; and functional aspects of organization of chromosome fibers. Molecular biologists, geneticists, scientists, and electron microscopists will find this book extremely helpful.
Author: Ronald E. Wrolstad
Publisher: John Wiley & Sons
ISBN: 0471709093
Category : Science
Languages : en
Pages : 1397
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Book Description
Emphasizing effective, state-of-the art methodology and written by recognized experts in the field, the Handbook of Food Analytical Chemistry is an indispensable reference for food scientists and technologists to enable successful analysis. * Provides detailed reports on experimental procedures * Includes sections on background theory and troubleshooting * Emphasizes effective, state-of-the art methodology, written by recognized experts in the field * Includes detailed instructions with annotated advisory comments, key references with annotation, time considerations and anticipated results
Author: Jack Kyte
Publisher: Garland Science
ISBN: 1136843507
Category : Science
Languages : en
Pages : 1576
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Book Description
The second edition of Structure in Protein Chemistry showcases the latest developments and innovations in the field of protein structure analysis and prediction. The book begins by explaining how proteins are purified and describes methods for elucidating their sequences of amino acids and defining their posttranslational modifications. Comprehensive explanations of crystallography and of noncovalent forces-ionic interactions, hydrogen bonding, and the hydrophobic effect-act as a prelude to an exhaustive description of the atomic details of the structures of proteins. The resulting understanding of protein molecular structure forms the basis for discussions of the evolution of proteins, the symmetry of the oligomeric associations that produce them, and the chemical, mathematical, and physical basis of the techniques used to study their structures. The latter include image reconstruction, nuclear magnetic resonance spectroscopy, proton exchange, optical spectroscopy, electrophoresis, covalent cross-linking, chemical modification, immunochemistry, hydrodynamics, and the scattering of light, X-radiation, and neutrons. These procedures are applied to study the folding of polypeptides and the assembly of oligomers. Biological membranes and their proteins are also discussed. Structure in Protein Chemistry, Second Edition, bridges the gap between introductory biophysical chemistry courses and research literature. It serves as a comprehensive textbook for advanced undergraduates and graduate students in biochemistry, biophysics, and structural and molecular biology. Professionals engaged in chemical, biochemical, and molecular biological research will find it a useful reference.
Author: Claude Balny
Publisher: Elsevier
ISBN: 9780444510990
Category : Medical
Languages : en
Pages : 414
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Book Description
This is the first book covering all aspects of high pressure biochemistry and biophysics of proteins. Hydrostatic pressure is a powerful tool for study of biological systems. As a thermodynamic parameter, hydrostatic pressure has been known for a century to act on biological materials in a similar, but not identical, way to temperature. However, pressure was disregarded for a long time by biochemists mainly because the basic concepts (and the thermodynamics) focused on the chemical reactions involved and because general ideas on what pressure can add to the understanding of the behaviour of proteins were lacking. In recent decades, technological progress in the field of physics has shown, along with parameters such as temperature and solvent conditions, that pressure can be used for more refined thermodynamic and kinetic descriptions of biological processes and regulation of biological systems. The effects of pressure on proteins, nucleoproteins and membranes have recently been reviewed and several proceedings books have been published.
Author: Hans Neurath
Publisher: Elsevier
ISBN: 0323162037
Category : Science
Languages : en
Pages : 719
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Book Description
The Proteins, Third Edition, Volume V discusses the unifying concepts of protein chemistry. This volume contains three chapters that cover specific protein classes, namely, glycoproteins and cyclopeptides. Chapter 1 deals first with the purification and characterization of the N- and O-linked glycosidic groups of glycoproteins. This chapter then describes the oligosaccharide catabolism and the roles of lysosomal hydrolases, and of functions of glycoproteins as mediated by their oligosaccharide groups. Chapter 2 begins with a detailed review of ultraviolet and visible spectroscopic techniques along with their basic principles, as well as theoretical calculations of peptide spectra. This chapter then considers absorption spectroscopy, optical rotary dispersion, and circular dichroism, followed by a discussion on the use of these methods on the secondary, tertiary, and quaternary structures of proteins in solution. Infrared and Raman spectroscopy and their applications to secondary structure analysis of proteins are also included in this chapter. Chapter 3 provides a critical review of naturally occurring and synthetic cyclopeptides, a unique group of molecules that include diverse biological compounds such as toxins, hormones, regulators of ion transport, and antibiotics. Organic chemists and researchers, teachers and undergraduate students will find this book invaluable.
Author: Vladimir N. Uversky
Publisher: Nova Publishers
ISBN: 9781600214042
Category : Circular dichroism
Languages : en
Pages : 382
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Book Description
Author: Graham Barrett
Publisher: Springer Science & Business Media
ISBN: 9400948328
Category : Science
Languages : en
Pages : 694
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Book Description
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.
Author: Jacinto Steinhardt
Publisher: Academic Press
ISBN: 1483220303
Category : Science
Languages : en
Pages : 404
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Book Description
Multiple Equilibria in Proteins covers the multiple interactions between small ions and molecules and a protein molecule. The book also deals with the physicochemical mechanisms of this interaction and the information about protein structure and the forces stabilizing that structure. The text discusses the mathematical description of complex formation, the thermodynamic analysis of binding data, and various theoretical models which can be used to describe the phenomena of small molecule-macromolecule interactions. The measurement of complex formation; the binding of neutral molecules; and hydrogen-ion equilibria are also considered. The book further tackles metal-ion binding; the binding of organic ions by proteins; as well as protein-protein interaction. Chemists and biochemists will find the book useful.
