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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.

Protein Physics: A Course of Lectures covers the most general problems of protein structure, folding and function. It describes key experimental facts and introduces concepts and theories, dealing with fibrous, membrane, and water-soluble globular proteins, in both their native and denatured states. The book systematically summarizes and presents the results of several decades of worldwide fundamental research on protein physics, structure, and folding, describing many physical models that help readers make estimates and predictions of physical processes that occur in proteins. New to this revised edition is the inclusion of novel information on amyloid aggregation, natively disordered proteins, protein folding in vivo, protein motors, misfolding, chameleon proteins, advances in protein engineering & design, and advances in the modeling of protein folding. Further, the book provides problems with solutions, many new and updated references, and physical and mathematical appendices. In addition, new figures (including stereo drawings, with a special appendix showing how to use them) are added, making this an ideal resource for graduate and advanced undergraduate students and researchers in academia in the fields of biophysics, physics, biochemistry, biologists, biotechnology, and chemistry. Fully revised and expanded new edition based on the latest research developments in protein physics Written by the world's top expert in the field Deals with fibrous, membrane, and water-soluble globular proteins, in both their native and denatured states Summarizes, in a systematic form, the results of several decades of worldwide fundamental research on protein physics and their structure and folding Examines experimental data on protein structure in the post-genome era

The contents of this volume derive loosely from an EMBO worksh9P held at EMBL (Heidelberg) towards the end of 1989. The topic of Patterns in Protein Sequence and Structure attracted a wide range of participants, from biochemists to computer scientists, and that diversity has, to some extent, remained in the contributions to this volume. The problems of interpreting biological sequence data are to an increasing extent forcing molecular biologists to learn the language of computers, including at times, even the abstruse language of the computer scientists themselves. While, on their side, the computer scientists have discovered a veritable honey-pot of real data on which to test their algorithms. This enforced meeting of two otherwise alien fields has resulted in some difficulties in communication and it was an aim of the EMBO workshop to help resolve these. By the end, most biologists at the meeting had, at least, heard the terms Dynamic Programming and Regular Expression while for their part the computer programmers began to realise that protein sequences might be more than simple Markov chains in a 20-letter alphabet. Thanks to the modern facilities at EMBL, the three day meeting was video-taped and from this a transcript was taken and offered to the speakers as the basis for a contribution to this volume.

An ultimate goal of modern biology is to understand how the genetic blueprint of cells(genotype)determinesthestructure,function,andbehaviorofalivingorganism (phenotype). At the center of this scienti?c endeavor is characterizing the bioch- ical and cellular roles of proteins, the working molecules of the machinery of life. A key to understanding of functional proteins is the knowledge of their folded str- tures in a cell, as the structures provide the basis for studying proteins'functions and functional mechanisms at the molecular level. Researchers working on structure determination have traditionally selected - dividual proteins due to their functional importance in a biological process or pa- way of particular interest. Major research organizations often have their own protein X-ray crystallographic or/and nuclear magnetic resonance facilities for structure - termination, which have been conducted at a rate of a few to dozens of structures a year. Realizing the widening gap between the rates of protein identi?cation (through DNA sequencing and identi?cation of potential genes through bioinformatics an- ysis) and the determination of protein structures, a number of large scienti?c init- tives have been launched in the past few years by government funding agencies in the United States, Europe, and Japan, with the intention to solve protein structures en masse, an effort called structural genomics. A number of structural genomics centers (factory-like facilities) have been established that promise to produce solved protein structures in a similar fashion to DNA sequencing.

Protein Physics is a lively presentation of the most general problems of protein structure, folding and function from the physics and chemistry perspective, based on lectures given by the authors. It deals with fibrous, membrane and, most of all, with the best studied water-soluble globular proteins, in both their native and denatured states. The major aspects of protein physics are covered systematically, physico-chemical properties of polypeptide chains; their secondary structures; tertiary structures of proteins and their classification; conformational transitions in protein molecules and their folding; intermediates of protein folding; folding nuclei; physical backgrounds of coding the protein structures by their amino acid sequences and protein functions in relation to the protein structure. The book will be of interest to undergraduate and graduate level students and researchers of biophysics, biochemistry, biology and material science. Designed for a wide audience of undergraduate and graduate students, as well as being a reference for researchers in academia and industry Covers the most general problems of protein structure, folding, and function and introduces the key concepts and theories Deals with fibrous, membrane and especially water-soluble globular proteins, in both their native and denatured states Summarizes and presents in a systematic form the results of several decades of world wide fundamental research on protein physics, structure and folding Examines experimental data on protein structure in the post-genome era

Amino acid sequence analysis is useful for the study of problems ranging from modifications of single molecules to complex networks and interactions of species. Many available amino acid sequences are providing the basis for various studies at the proteome level.The dynamics of protein expression and the simulation of complex biological systems in which proteins interact with certain kinetics and in their respective compartments are just about to be tackled. Amino acid sequences will be crucial reference points for such studies.Key Features• Mass spectrometric analysis of proteins• Protein sequence databases• Amino acid substitution matrices• Amino acid-based phylogeny and alignment• Individual variation in protein-coding sequences of the human genome• Identifying nature's protein Lego(r) set

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.

The Peptides: Analysis, Synthesis, Biology: Volume 4: Modern Techniques of Conformational, Structural, and Configurational Analysis is an open-ended treatise that provides comprehensive and critical reviews of important developments in all areas of peptide research including analysis, synthesis, and biology. X-ray structure studies, amino acid analysis, and chiroptical analysis of configuration are discussed, along with solid-phase sequencing and ultramicroanalysis with the aid of fluorescence. This volume is comprised of six chapters and begins with an account of crystal structure analysis on molecules containing 2-12 peptide units, focusing on the variety of intramolecular hydrogen bonds, cis peptide units, and multiple conformation. Conformational changes upon complexation with metal ions are considered, together with the inclusion of solvents as integral parts of a molecular structure. The following chapters explore the conformations of insulin, glucagon, pancreatic polypeptide and related molecules, as well as the molecular biology of these hormones based on crystal structures; the usefulness of chiroptical techniques for determining the absolute configuration of amino acids and small peptides; and ultramicroanalysis of peptides and proteins by high performance liquid chromatography and fluorescence detection. The final chapter looks at the status and future potential of solid-phase sequencing. This book is intended as a reference for specialists, a guide for the novice, and a forum for investigators concerned with research on peptides and proteins.

Techniques in Protein Chemistry VI, an invaluable bench-top reference source for protein chemists, highlights current methods in the following areas: 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 Analysis of protein interactions Protein design and engineeringTechniques in Protein Chemistry VI, an invaluable bench-top reference source for protein chemists, highlights current methods in the following areas: 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 Analysis of protein interactions Protein design and engineering

The first of its kind, Introduction to Biophysical Methods for Protein and Nucleic Acid Research serves as a text for the experienced researcher and student requiring an introduction to the field. Each chapter presents a description of the physical basis of the method, the type of information that may be obtained with the method, how data should be analyzed and interpreted and, where appropriate, practical tips about procedures and equipment.Key Features• Modern Use of Mass Spectroscopy• NMR Spectroscopy• Molecular Modeling and Graphics• Macintosh and DOS/Windows 3.x disks