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.

Current Research in Protein Chemistry: Techniques, Structure, and Function reviews new techniques and methods for determining the structure and function of proteins. Topics covered include protein folding and stability, chimeric proteins, amino acid and peptide analysis, mass spectrometric methods, and protein sequencing techniques. This book is divided into six sections comprised of 55 chapters. The discussion begins with a description of microwave irradiation that uses Teflon-Pyrex tubes for protein hydrolysis, followed by the application of high performance capillary electrophoresis to the analysis of amino acids. The sections that follow explore mass spectrometry, protein sequencing, and capillary electrophoresis as well as protein stability, chimeric proteins and enzyme modifications, and protein structure prediction. Chapters focus on the crystal structure of human interleukin-1a, the acid-denatured states of proteins, solubility of recombinant proteins expressed in Escherichia coli, and catalysis by chimeric proteins. This book will be of value to students and researchers interested in 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.

In recent years, interest in proteins has surged. This resurgence has been driven by the expansion of the post-genomic era when structural genomics and proteomics require new techniques in protein chemistry and new applications of older techniques. Protein chemistry methods are used by nearly every discipline of biomedical research. Many techniques

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.

Bioconjugate Techniques, 2nd Edition, is the essential guide to the modification and cross linking of biomolecules for use in research, diagnostics, and therapeutics. It provides highly detailed information on the chemistry, reagent systems, and practical applications for creating labeled or conjugate molecules. It also describes dozens of reactions with details on hundreds of commercially available reagents and the use of these reagents for modifying or cross linking peptides and proteins, sugars and polysaccharides, nucleic acids and oligonucleotides, lipids, and synthetic polymers. A one-stop source for proven methods and protocols for synthesizing bioconjugates in the lab Step-by-step presentation makes the book an ideal source for researchers who are less familiar with the synthesis of bioconjugates More than 600 figures that visually describe the complex reactions associated with the synthesis of bioconjugates Includes entirely new chapters on the latest areas in the field of bioconjugation as follows: Microparticles and nanoparticlesSilane coupling agentsDendrimers and dendronsChemoselective ligationQuantum dotsLanthanide chelatesCyanine dyesDiscrete PEG compoundsBuckyballs,fullerenes, and carbon nanotubesMass tags and isotope tagsBioconjugation in the study of protein interactions

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 V highlights current methods in peptide and protein mass spectrometry, sequence and amino acid analysis, fragmentations, separations, protein folding and modeling, peptide and protein NMR, and peptide synthesis. This volume emerged from the manuscripts presented at the Seventh Symposium of the Protein Society, held in San Diego on July 24-28, 1993. This volume is organized into eight parts encompassing 61 chapters. The first part surveys the peptide and protein characterization, detection, and analysis by mass spectrometry. The subsequent parts describe the structural characterization and analysis of posttranslational processing events, as well as the characterization of protein and amino acid sequences using several analytical techniques. Other parts explore other analytical methods for peptide and protein separations; some aspects involved in protein design and functional domain analysis; and the evaluation of protein conformation, folding, and modeling. The last parts contain research papers on NMR analysis of peptide and protein solution structures. These parts also look into topics related to peptide synthesis and peptide libraries. This book is intended primarily for protein and analytical chemists.

Techniques in Protein Chemistry IV compiles papers presented at the Sixth Protein Society Symposium held in San Diego, California in 1992. This book discusses the mass spectrometry in protein sequence and structural investigations; site specific heterogeneity of N-linked oligosaccharides on recombinant human erythropoietin; and modification of thiophosphorylated proteins with extrinsic probes. The cysteine and tryptophan amino acid analysis of ABRF92-AAA; development of separation strategies for proteins by capillary electrophoresis; and peptide mapping of 2-D gel proteins by capillary HPLC are also elaborated. This text likewise covers the single syringe-pump solid-phase protein sequencer; hydrophobic contact density distribution functions; and application of chemical shift calculation to protein structure determination by NMR. This publication is valuable to biologists and students concerned with the developments in mass spectrometry of proteins.

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.