Functional Disulphide Bonds Methods and Protocols
This book describes the current techniques used to study functional disulphides and to exploit them for therapeutic outcomes. Beginning with how disulphide bonds are classified and how to study their evolution, the volume then continues with protein chemi
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Philip Hogg Editor
Functional Disulphide Bonds Methods and Protocols
METHODS
IN
MOLECULAR BIOLOGY
Series Editor John M. Walker School of Life and Medical Sciences University of Hertfordshire Hatfield, Hertfordshire, AL10 9AB, UK
For further volumes: http://www.springer.com/series/7651
Functional Disulphide Bonds Methods and Protocols
Edited by
Philip Hogg The Centenary Institute, NHMRC Clinical Trials Centre, Sydney Medical School, University of Sydney, Sydney, NSW, Australia
Editor Philip Hogg The Centenary Institute, NHMRC Clinical Trials Centre Sydney Medical School University of Sydney Sydney, NSW, Australia
ISSN 1064-3745 ISSN 1940-6029 (electronic) Methods in Molecular Biology ISBN 978-1-4939-9186-0 ISBN 978-1-4939-9187-7 (eBook) https://doi.org/10.1007/978-1-4939-9187-7 © Springer Science+Business Media, LLC, part of Springer Nature 2019 This work is subject to copyright. All rights are reserved by the Publisher, whether the whole or part of the material is concerned, specifically the rights of translation, reprinting, reuse of illustrations, recitation, broadcasting, reproduction on microfilms or in any other physical way, and transmission or information storage and retrieval, electronic adaptation, computer software, or by similar or dissimilar methodology now known or hereafter developed. The use of general descriptive names, registered names, trademarks, service marks, etc. in this publication does not imply, even in the absence of a specific statement, that such names are exempt from the relevant protective laws and regulations and therefore free for general use. The publisher, the authors, and the editors are safe to assume that the advice and information in this book are believed to be true and accurate at the date of publication. Neither the publisher nor the authors or the editors give a warranty, express or implied, with respect to the material contained herein or for any errors or omissions that may have been made. The publisher remains neutral with regard to jurisdictional claims in published maps and institutional affiliations. This Humana Press imprint is published by the registered company Springer Science+Business Media, LLC part of Springer Nature. The registered company address is: 233 Spring Street, New York, NY 10013, U.S.A.
Preface Disulfide bonds are the covalent links between the sulfur atoms of pairs of cysteine amino acids in the polypeptide chain. They are the second most common covalent bond linking the polypeptide backbone after the peptide bond. For several decades, disulphide bonds were thought to be inert in the mature protein. We know now that a subset of disulfide bonds control the function of the mature protein in which they reside when cleaved and/or formed by different factors. These allosteric disulphides and the factors that cleave them have been shown to control protein function across biological systems and life-forms. This book describes the current techniques used to study this post-translational modification and to exploit it for therapeutic outcomes
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