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Much of the recent spectacular progress in the biological sciences can be at tributed ot the ability to isolate, analyze, and structurally characterize proteins and peptides which are present in cells and cellular organelles in only very small amounts. Recent advances in protein chemistry and in particular the application of new micromethods have led to fruitful advances in the understanding of basic cellular processes. Areas where protein-chemical studies have resulted in interest ing discoveries include the peptide hormones and their release factors, growth factors and oncogenes, bioenergetics, proton pumps and ion pumps and chan nels, topogenesis and protein secretion, molecular virology and immunology, membrane protein analysis, and receptor research. In fact, the key methods are now on hand to unravel many of the major outstanding problems of molecular biology and in particular questions of fundamental interest which relate to devel opmental biology and specificity in cell-cell interaction. In this volume we have assembled descriptions of procedures which have re cently been shown to be efficaceous for the isolation, purification, and chemical characterization of proteins and peptides that are only available in minute amounts. Emphasis is placed on well-established micromethods which have been tested and found useful in many laboratories by experienced investigators. The chapters are written by specialists, and describe a range of sensitive techniques which can be used by researchers working in laboratories with only modest resources and equipment.
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This book is an attempt to provide in a single source current state-of-the-art methodologies for protein sequence analysis. It is hoped that these various chapters are presented in such a way that both the newcomer and the established protein chemist will find useful information and directions to new techniques. This book offers a rich array of techniques and methods for sequencing proteins and peptides. It should meet the expectations of investigators in protein chemistry who wish to update their knowledge of sequencing techniques, and of those who wish to reacquaint themselves with the best available current technologies.
"Methods in Protein Sequence Analysis - 1988" - contains selected contributions on modern protein- analytical techniques as presented by speakers at the Seventh International Conference on "Methods in Protein Sequence Analysis", held from July 3rd to July 8th, 1988 in Berlin. The book contains information on new methodologies for sensitive amino acid analysis, N- and C-terminal sequence analysis, and protein and peptide purification. In addition recent mass spectrometric approaches are described, as an alter native technique to the common stepwise degradative sequence analysis of polypeptides by the Edman method. The book presents new possibilities in the design of sequencers and sophisticated equipment for the structural analysis of peptides and proteins. It describes practical approaches for the investigation of protein domains and protein complexes, and contains review chapters on the crystallization of cell organelles as well as on recent theoretical aspects of protein folding mechanisms. The nature of protein folding is not yet understood, but further advances in this area would greatly enhance our present knowledge of protein structure and function. Further, the book gives examples of the application of gene technology to protein characterization and to the design of new proteins. This enables new studies on the structure and function of proteins to be made, and opens up efficient approaches to the design of drugs.
The Ninth International Conference on Methods in Protein Sequence Analysis was held for the first time in Asia from September 20 to September 24, 1992 in Otsu (a city near Kyoto), Japan. Approximately 400 delegates attended the meeting. Forty papers were presented orally and 147 poster presentations were discussed. Academic sessions were held from early in the morning until late in the evening. We are confident that the Conference was successful in providing up-to-date information about methods in protein sequence analysis to all participants. Moreover, with the knowledge and understanding of the present standard of various methods of analysis that are being used and will be used, we were able to clarify areas that need to be evaluated, to be improved and be explored further. Major topics in the Conference mostly covered areas in the methodology of protein sequence analysis, such as: micropreparation and microsequencing of proteins, mass spectrometry, post-translational modification, prediction and database analysis, and analysis of protein structures of special interests. The evolution of genetic engineering in molecular biology has greatly accelerated the accumulation of knowledge on the amino acid sequence of novel proteins regardless of whether they are expressed or not expressed in living organisms. In the early stage of accumulation of structural information, the amino acid sequence itself is worthy of notice.
Methods in protein sequence analysis constitute important fields in rapid progress. We have experienced a continuous increase in analytical sensitivity coupled with decreases in time necessary for purification and analysis. Several generations of sequencers, liquid/solid/gas-phase, have passed by and returned in other shapes during just over two decades. Similarly, the introduction of HPLC permitted an enormous leap forward in this as in other fields of biochemistry, and we now start to see new major advances in purification/analysis through capillary electrophoresis. Furthermore, progress in the field of mass spectrometry has matched that in chemical analysis and we witness continuous development, now emphasizing ion spray and other mass spectrometric approaches. In short, protein analysis has progressed in line with other developments in modern science and constitutes an indispensable, integral part of present-day molecular biology. Even the available molecular tools, in the form of proteases with different specificities, have increased in number, although we still have far to go to reach an array of "restriction proteases" like the sets of nucleases available to the molecular geneticist. Of course, conferences have been devoted to protein sequence analysis, in particular the MPSA (Methods in Protein Sequence Analysis) series, of which the 8th conference took place in Kiruna, Sweden, July 1-6 1990. Again, we witnessed much progress, saw new instruments, and experienced further interpretational insights into protein mechanisms and functions.
Why a Second Edition?The Second Edition provides practical answers to the general question, "How can I obtain useful sequence information from my protein or peptide?" rather than the more specific question asked in the first edition, "How can I obtain the N-terminal sequence?" Important new methods include ways of dealing with blocked N termini, computer analysis of protein sequences, and the recent revolution in mass spectrometry. - Mass spectrophotometric characterization of proteins and peptides - N-terminal sequencing of proteins with blocked N termini - Internal amino acid sequence analysis after protease digestion in-gel and on-blot - Improved microscale peptide purification methods - Computer analysis of protein sequences - New protocols tested and refined through everyday use in authors' laboratories - Updated reference chapter covering all aspects of protein microsequencing
"Protein Structure Analysis - Preparation and Characterization" is a compilation of practical approaches to the structural analysis of proteins and peptides. Here, about 20 authors describe and comment on techniques for sensitive protein purification and analysis. These methods are used worldwide in biochemical and biotechnical research currently being carried out in pharmaceu tical and biomedical laboratories or protein sequencing facilities. The chapters have been written by scientists with extensive ex perience in these fields, and the practical parts are well documen ted so that the reader should be able to easily reproduce the described techniques. The methods compiled in this book were demonstrated in student courses and in the EMBO Practical Course on "Microsequence Analysis of Proteins" held in Berlin September 10-15, 1995. The topics also derived from a FEBS Workshop, held in Halkidiki, Thessaloniki, Greece, in April, 1995. Most of the authors participated in these courses as lecturers and tutors and made these courses extremely lively and successful. Since polypeptides greatly vary depending on their specific structure and function, strategies for their structural analysis must for the most part be adapted to each individual protein. Therefore, advantages and limitations of the experimen tal approaches are discussed here critically, so that the reader becomes familiar with problems that might be encountered.
Methods in Protein Sequence Analysis -1986 brings together reports of the most recent methodology available to protein chemists for studying the molecular detail of proteins. The papers in this volume constitute the proceedings of the Sixth International Conference on Methods in Protein Sequence Analysis, which was held at the University of Washington in Seattle, Washington on August 17-21, 1986. This series of conferences has taken place during a period when new techniques in protein chemistry and molecular biology have enabled not only exploration of the control of protein function, but also deduction of the genetic origin of proteins, and labo ratory generation of rare protein molecules for therapeu tic and commercial use. The current reports are focused on the means by which experimental questions can be answered rather than on the biological implications in specific systems. The scope of the meeting was quite broad, empha sizing microanalytical techniques and the relative merits of DNA sequencing, mass spectrometry and more tradi tional degradation techniques. A highlight of the meeting was the Qrowing awareness of the role of mass spec trometry In the analysis of proteins. The complementarity of protein sequencing and DNA sequencing techniques was apparent throughout the discussions and several papers dealt with the strategy of obtaining sequence in formation from small amounts of protein in order that ap propriate oligonucleotide probes could be constructed and the encoding nucleic acids se. quenced and manipu lated.
Proteins are the servants of life. They occur in all com- nent parts of living organisms and are staggering in their fu- tional variety, despite their chemical similarity. Even the simplest single-cell organism contains a thousand different p- teins, fulfilling a wide range of life-supporting roles. Additions to the total number of known proteins are being made on an increasing scale through the discovery of mutant strains or their production by genetic manipulation. The total international protein literature could fill a medi- sized building and is growing at an ever-increasing rate. The reader might be forgiven for asking whether yet another book on proteins, their properties, and functions can serve a useful purpose. An explanation of the origin of this book may serve as justification. The authors form the tutorial team for an int- sive postexperience course on protein characterization or- nized by the Center for Professional Advancement, East Brunswick, New Jersey, an educational foundation. The course was first mounted in Amsterdam in 1982 and has since been repeated several times, in both Amsterdam and the US, with participants from North America and most European countries. In a predecessor to this book, emphasis was placed on the role of protein isolation in the food industry, because at the time this reflected the interests of most of the participants at the course. Today, isolated proteins for food use are extracted from yeasts, fungal sources, legumes, oilseeds, cereals, and leaves.