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Techniques in Protein Chemistry VII, a valuable bench-top reference tool for protein chemists, features the most up-to-date advances in protein methodologies. Key Features * Protein sequencing and amino acid analysis * Mass spectral analysis of peptides and proteins * Posttranslational processing * High-sensitivity protein and peptide separations * Protein folding and NMR * Functional domain analysis * Protein design and engineering
Techniques in Protein Chemistry III compiles papers presented at the Fifth Protein Society Symposium in Baltimore on June 22-26, 1991. This book discusses the protein and peptide recovery from PVDF membranes; high-sensitivity peptide mapping utilizing reversed-phase microbore and microcolumn liquid chromatography; and capillary electrophoresis for preparation of peptides and direct determination of amino acids. The TFMSA/TFA cleavage in t-Boc peptide synthesis; applications of automatic PTC amino acid analysis; and identification of O-glycosylation sites with a gas phase sequencer are also elaborated. This text likewise covers the conformational stability of the molten globule of cytochrome c and role of aqueous solvation in protein folding. This publication is useful to students and researchers interested in methods and research approaches on protein chemistry.
This book presents a survey of recent developments in protein biochemistry. Top researchers in the field of protein biochemistry describe modern methods to address the challenges of protein purification by three-phase partitioning, and their folding and degradation by the functions of chaperones. The significance of peptide purity for fibril formation is addressed as well as the use of target oriented peptide arrays in palliative approaches in mucoviszidose. The design and application of protein epitope mimetics just as the structural resolving of the misfolding of various mutant proteins in serpinopathies enlarge our tools in resolving pathophysiological imbalances.
Techniques in Protein Chemistry compiles reports of methods and techniques presented at the second symposium of the Protein Society in August 1988. This book includes methods and applications in protein sequencing, advanced applications of mass spectrometry and nuclear magnetic resonance technology, limitations of amino acid microanalysis, and advances in high-performance liquid chromatography. The structure of synthetic test peptide-3 (STP-3), a peptide designed to test the analytical limits of current technology in the field of protein chemistry is also elaborated. This publication is suited for chemists and researchers conducting work on the analytical techniques available for the molecular characterization of proteins.
This class-tested textbook gives an overview of the structure and functions of proteins and explains how amino acids form a defined structural entity with specific properties. The authors also introduce modern methods for purification and separation of proteins as well as different techniques for analyzing their structural and functional properties. A separate part of the book is devoted to enzymes and kinetics of enzymatic reactions.
Techniques in Protein Chemistry VII is the latest in a highly successful chronicle of the most recent developments in proteins. The contributions were selected from presentations at the Ninth Symposium of the Protein Society held in Boston, Massachusetts in July 1995.
Hormonal Proteins and Peptides: Techniques in Protein Chemistry, Volume IX presents the various methods in protein chemistry and discusses their use for hormonal protein investigations. This book examines the approach to investigating biologically active peptides, which is based on a combination of chromatographic and fluorometric procedures. 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.
The Protein Protocols Handbook, Second Edition aims to provide a cross-section of analytical techniques commonly used for proteins and peptides, thus providing a benchtop manual and guide for those who are new to the protein chemistry laboratory and for those more established workers who wish to use a technique for the first time. All chapters are written in the same format as that used in the Methods in Molecular BiologyTM series. Each chapter opens with a description of the basic theory behind the method being described. The Materials section lists all the chemicals, reagents, buffers, and other materials necessary for carrying out the protocol. Since the principal goal of the book is to provide experimentalists with a full account of the practical steps necessary for carrying out each protocol successfully, the Methods section contains detailed st- by-step descriptions of every protocol that should result in the successful execution of each method. The Notes section complements the Methods material by indicating how best to deal with any problem or difficulty that may arise when using a given technique, and how to go about making the widest variety of modifications or alterations to the protocol. Since the first edition of this book was published in 1996 there have, of course, been significant developments in the field 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.