Folding of Disulfide Proteins
Disulfide-containing proteins belong to a unique class of proteins for studying the mechanism of protein folding. Their folding mechanism can be analyzed by three distinct techniques: (1) The conventional denaturation-renaturation method (disulfide intact
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Rowen J.Y. Chang • Salvador Ventura Editors
Folding of Disulfide Proteins
Editors Rowen J.Y. Chang Research Center for Protein Chemistry Brown Foundation Inst. of Molecular Medicine, Dept. of Biochemistry and Molecular Biology The University of Texas Houston, TX 77030, USA [email protected]
Salvador Ventura Dept. de Bioquímica i Biologia Molecular Institut de Biotecnologia i de Biomed. Universitat Autònoma de Barcelona Bellaterra-08193, Spain [email protected]
ISBN 978-1-4419-7272-9 e-ISBN 978-1-4419-7273-6 DOI 10.1007/978-1-4419-7273-6 Springer New York Dordrecht Heidelberg London Library of Congress Control Number: 2011932496 © Springer Science+Business Media, LLC 2011 All rights reserved. This work may not be translated or copied in whole or in part without the written permission of the publisher (Springer Science+Business Media, LLC, 233 Spring Street, New York, NY 10013, USA), except for brief excerpts in connection with reviews or scholarly analysis. Use in connection with any form of information storage and retrieval, electronic adaptation, computer software, or by similar or dissimilar methodology now known or hereafter developed is forbidden. The use in this publication of trade names, trademarks, service marks, and similar terms, even if they are not identified as such, is not to be taken as an expression of opinion as to whether or not they are subject to proprietary rights. Printed on acid-free paper Springer is part of Springer Science+Business Media (www.springer.com)
Preface
The formation of selected intramolecular disulfide bonds is one of the most important postraductional modifications of proteins, influencing their folding, stability, and biological function. The folding of disulfide proteins is usually an intricate process in which, after their synthesis at the ribosome in a reduced and unfolded state, polypeptides gain coordinately their native disulfide bonds as well as their unique and stable conformation. In the cell, this process is exquisitely controlled and catalyzed by a complex protein machinery to avoid mispairing of cysteine residues, which might prevent the attaining of functional conformations leading to misfolding and, in some cases, triggering pathological processes. In vitro, the folding of disulfide proteins has constituted the bedrock for a long time on which to understand at the kinetic and structural levels the mechanisms by which a particular amino acid chain folds into a specific functional conformation. The aim of the present monograph is to provide the reader with a detailed view of our current structural and functional understanding of the complex process of protein oxidative folding and of their chemical, biotechnological, and biomedical implications; together with a historical perspective of a field that this year 2011 celebrates its 50th anniversary. The book presents a comprehensive description of the complexity and diversity of folding pathways of different disulfide protein models, i
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