Molecular Chaperones Methods and Protocols
The proteome consists of a complex mixture of proteins each of which need to be folded correctly in order to function for the health of the organism, and many of these proteins require molecular chaperones to reach the correct conformation and, in some ca
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Molecular Biology™
Series Editor John M. Walker School of Life Sciences University of Hertfordshire Hatfield, Hertfordshire, AL10 9AB, UK
For further volumes: http://www.springer.com/series/7651
Molecular Chaperones Methods and Protocols
Edited by
Stuart K. Calderwood Molecular and Cellular Radiation Oncology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA, USA
Thomas L. Prince Urologic Oncology Branch, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA
Editors Stuart K. Calderwood, Ph.D. Molecular and Cellular Radiation Oncology Beth Israel Deaconess Medical Center Harvard Medical School Boston, MA USA [email protected]
Thomas L. Prince Urologic Oncology Branch National Cancer Institute National Institutes of Health Bethesda, MD USA [email protected]
ISSN 1064-3745 e-ISSN 1940-6029 ISBN 978-1-61779-294-6 e-ISBN 978-1-61779-295-3 DOI 10.1007/978-1-61779-295-3 Springer New York Dordrecht Heidelberg London Library of Congress Control Number: 2011934798 © 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 (Humana Press, c/o 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 Humana Press is part of Springer Science+Business Media (www.springer.com)
Dedication I would like to dedicate the book to my beautiful wife Laura and to the memory of my mother and father Albert and Gwyneth Calderwood.
Preface The proteome consists of a complex mixture of proteins each of which need to be folded correctly for their function and for the health of the organism. Many of these proteins require molecular chaperones to reach the correct conformation and in some cases to remain in a folded form. Although many proteins fold spontaneously under in vitro conditions, under the crowded confines of the cell these molecular chaperones are required to prevent loss of function and aggregation [1–3]. Proteome quality is mediated by a number of mechanisms, including facilitated folding by the chaperones, degradation of the protein, or disposal of aggregates by asynchronous cell division. Cells have a repertoire of folding molecules consisting of multiple cohorts of molecular chaperones with subtly different properties in the protein quality control pathways. Under some conditions, such as heat shock, protein unfolding reaches crisis conditions and overwhelms these quality control m
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