These still remain valuable techniques and receive appropriate coverage in this book. From the beginning, the cornerstone of proteomics has been the use of twodimensional gel electrophoresis to compare proteomes of different tissues (for example, normal and diseased tissue) with the subsequent identification of protein differences by the use of mass spectrometry and database searching. However, the wealth of gene sequencing data now available has produced a glut of information that challenges the protein chemist to develop new tools to utilize this flood of genomic data. The focus of attention has therefore turned to directly examining these protein components as the means of understanding cell function, as well as the cellular changes involved in disease states. For a variety of reasons (including alternative mRNA splicing, varying translational stop/start sites, frameshifting, and the inability to deduce posttranslational modifications), complete sequences of genomes are insufficient to elucidate the protein components of cells. The completion of the sequences of an ever-widening range of genomes-not least of all, the human genome-has provided the molecular biologist with a wealth of data that needs to be analyzed and interpreted.
At the basic research level, phenotype will be explained in terms of cellular mechanisms.
The subsequent increased understanding of the mechanisms of cellular function and misfunction will have particular impact in the area of medical research, where disease processes will be better understood, many new (protein) therapeutic targets identified, and novel therapeutic agents developed. Preface Recent developments in the field of proteomics have revolutionized the way that proteins, and their contribution to cellular functions, are studied. Includes bibliographical references and index. 10 9 8 7 6 5 4 3 2 1 e-ISBN: 1-59259-890-0 Library of Congress Cataloging in Publication Data Proteomics protocols handbook / edited by John M.
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