Photoaffinity Labeling for Structural Probing Within Protein
This book covers the most up-to-date photoaffinity labeling method to tackle the key loop module involved in the binding process of a bioactive small molecule to its host protein. The book introduces rational points for preparing powerful photoaffinity pr
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hotoaffinity Labeling for Structural Probing Within Protein
Photoaffinity Labeling for Structural Probing Within Protein
Yasumaru Hatanaka • Makoto Hashimoto Editors
Photoaffinity Labeling for Structural Probing Within Protein
Editors Yasumaru Hatanaka University of Toyama Toyama Japan
Makoto Hashimoto Graduate School of Agriculture Hokkaido University Sapporo Hokkaido Japan
ISBN 978-4-431-56568-0 ISBN 978-4-431-56569-7 (eBook) DOI 10.1007/978-4-431-56569-7 Library of Congress Control Number: 2017954302 © Springer Japan KK 2017 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. Printed on acid-free paper This Springer imprint is published by Springer Nature The registered company is Springer Japan KK The registered company address is: Chiyoda First Bldg. East, 3-8-1 Nishi-Kanda, Chiyoda-ku, Tokyo 101-0065, Japan
Foreword
Harnessing the Protein The highly ordered molecular assembly of living systems represents an endless frontier for the application of chemical biology. A useful chemical approach to define specific molecular recognition is covalent cross-linking of a ligand and its receptor in an affinity-based manner. The chemical basis for affinity cross-linking is classified into two categories: ground-state reactions secure the residue-selective nature of affinity labeling and excited-state reactions generate highly reactive species to characterize the powerful feature of photoaffinity labeling. The major advantage for photoaffinity labeling is that the probe is inert before irradiation to prevent ground-state side reactions with surrounding molecules in a non-specific manner. Ideally, the irradiation immediately generates an extremely reactive species to complete specific and stable cross-links which comes in contact with any one of the residues located close by. Since Frank H. Westheimer originally introduced this unique idea of the method in
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