Allostery Methods and Protocols
Despite considerable variability within the scientific community, allosteric regulation can best be defined functionally as how a macromolecule binds one ligand differently when a second ligand is or is not pre-bound to the macromolecule, which constitute
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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
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Allostery Methods and Protocols
Edited by
Aron W. Fenton Department of Biochemistry and Molecular Biology, The University of Kansas Medical Center, Kansas City, KS, USA
Editor Aron W. Fenton Department of Biochemistry and Molecular Biology The University of Kansas Medical Center Kansas City, KS, USA [email protected]
ISSN 1064-3745 e-ISSN 1940-6029 ISBN 978-1-61779-333-2 e-ISBN 978-1-61779-334-9 DOI 10.1007/978-1-61779-334-9 Springer New York Dordrecht Heidelberg London Library of Congress Control Number: 2011938679 # Springer ScienceþBusiness Media, LLC 2012
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 ScienceþBusiness 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 a part of Springer Science+Business Media (www.springer.com)
Dedication I am convinced that all that is in the Universe revolves around my amazing wife; without her efforts, I could not do science. I have been in the fortunate position to have been trained by three mentors who are not only good people, but also believe in science at the highest caliber. Therefore, I would like to dedicate this book to these four individuals: Shellee Fenton and Drs. James B. Blair, Gregory D. Reinhart, and Gerald M. Carlson.
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Preface In the past 7 years, allostery has resurfaced as a major focus in understanding protein structure/function. Much of this rejuvenated interest has been driven by the ability of NMR to monitor protein dynamics and the potential of determining how these dynamics contribute to protein functions, including allostery (1–6). A second driving force for the recent interest is a growing appreciation that allosteric drugs offer safety advantages over conventional drugs (7–9). This renewed interest has resulted in several reviews on allostery (10–13). At the onset of any discussion on allostery, it is beneficial to review the exact phenomenon included in the discussion. Shortly after the original use of “allosteric” (14), confusion over the definition of this term showed up in the literature. One source of confusion is whether “allostery” and “cooperative” should be treated as two synonyms to describe the same principle or if these words describe two different phenomen
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