Protein Amyloid Aggregation Methods and Protocols
This detailed volume focuses on methods for the characterization of aggregation processes that lead to the formation of amyloid fibrils and amyloid oligomers which feature in the etiology of a variety of human disorders collectively known as amyloidoses.
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David Eliezer Editor
Protein Amyloid Aggregation 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
Protein Amyloid Aggregation Methods and Protocols
Edited by
David Eliezer Weill Cornell Medical College, New York, NY, USA
Editor David Eliezer Weill Cornell Medical College New York, NY, USA
ISSN 1064-3745 ISSN 1940-6029 (electronic) Methods in Molecular Biology ISBN 978-1-4939-2977-1 ISBN 978-1-4939-2978-8 (eBook) DOI 10.1007/978-1-4939-2978-8 Library of Congress Control Number: 2015949999 Springer New York Heidelberg Dordrecht London © Springer Science+Business Media New York 2016 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. Printed on acid-free paper Humana Press is a brand of Springer Springer Science+Business Media LLC New York is part of Springer Science+Business Media (www.springer.com)
Preface This volume is focused on methods for the characterization of aggregation processes that lead to the formation of amyloid fibrils and amyloid oligomers that feature in the etiology of a variety of human disorders collectively known as amyloidoses. The focus includes techniques for visualizing early steps on the amyloid formation pathway, methods for capturing and characterizing oligomeric, potentially toxic, intermediates, strategies for preparing and characterizing mature amyloid fibrils, and approaches for understanding templating and transmission of amyloid aggregates. The target audience includes biochemists and biophysicists with an interest in elucidating the mechanisms of protein amyloid formation, as well as chemists, pharmacologists, and clinicians with an interest in leveraging an understanding of such mechanisms for the purpose of therapeutic development. Chapter 1 treats methods to prepare posttranslationally modified amyloid proteins with a focus on the productio
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