Amyloid Proteins Methods and Protocols
Amyloid diseases are characterized by the deposition of insoluble fibrous amyloid proteins. The word “amyloid” indicates a starch-like compound, and though a misnomer, continues to be the accepted term for this group of protein conformational disorders. T
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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
Amyloid Proteins Methods and Protocols
Second Edition Edited by
Einar M. Sigurdsson Departments of Physiology and Neuroscience, and Psychiatry, School of Medicine, New York University, New York, NY, USA
Miguel Calero Centro Nacional de Microbiología, Instituto de Salud Carlos III, Majadahonda, Madrid, Spain
María Gasset Instituto de Química-Física Rocasolano, CSIC, Madrid, Spain
Editors Einar M. Sigurdsson Departments of Physiology and Neuroscience, and Psychiatry School of Medicine New York University New York, NY, USA
Miguel Calero Centro Nacional de Microbiología Instituto de Salud Carlos III Majadahonda, Madrid, Spain
María Gasset Instituto de Química-Física Rocasolano CSIC, Madrid, Spain
ISSN 1064-3745 e-ISSN 1940-6029 ISBN 978-1-61779-550-3 e-ISBN 978-1-61779-551-0 DOI 10.1007/978-1-61779-551-0 Springer New York Dordrecht Heidelberg London Library of Congress Control Number: 2012930138 © Springer Science+Business 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 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. Cover illustration: The cover art depicts fibers assembled from full-length Tau and observed by Atomic Force Microscopy. Courtesy of Susanne Wegmann (D. Müller laboratory, ETHZ Basel, Switzerland). Printed on acid-free paper Humana Press is part of Springer Science+Business Media (www.springer.com)
Preface Amyloid diseases are characterized by the deposition of insoluble fibrous amyloid proteins. The word “amyloid” indicates a starch-like compound, and though a misnomer, continues to be the accepted term for this group of protein conformational disorders. Approximately 30 different proteins can form amyloid and although there is usually no homology in their amino acid sequence, all share a β-pleated sheet as the polymer scaffold. Historically, these β-pleated deposits were detected by histological dyes, and the characteristic fibril structure confirmed with electron microscopy. As these amyloids were purified and sequenced, various in vitro techniques were developed, often using synthetic peptides and/or highly purified amyloids derived from diseased tissue. Development of animal models occurred concurrently and some of these diseases can now
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