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Methods in Molecular Biology

Protein Amyloid Aggregation

Methods and Protocols

Editors: Eliezer, David (Ed.)

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  • Includes cutting-edge methods and protocols for studying protein amyloid aggregation
  • Provides step-by-step detail essential for reproducible results
  • Contains key notes and implementation advice from the experts
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  • ISBN 978-1-4939-2978-8
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Hardcover $169.99
price for USA in USD
  • ISBN 978-1-4939-2977-1
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Softcover $139.99
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  • ISBN 978-1-4939-5005-8
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  • Institutional customers should get in touch with their account manager
  • Covid-19 shipping restrictions
  • Usually ready to be dispatched within 3 to 5 business days, if in stock
About this book

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. The scope of the collection 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. Written in the highly successful Methods in Molecular Biology series format, the chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols and tips on troubleshooting and avoiding known pitfalls.

Authoritative and practical, Protein Amyloid Aggregation: Methods and Protocols serves as an ideal guide for 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.

Table of contents (20 chapters)

Table of contents (20 chapters)
  • Semisynthesis and Enzymatic Preparation of Post-translationally Modified α-Synuclein

    Pages 3-20

    Fauvet, Bruno (et al.)

  • Isotope-Labeled Amyloids via Synthesis, Expression, and Chemical Ligation for Use in FTIR, 2D IR, and NMR Studies

    Pages 21-41

    Zhang, Tianqi O. (et al.)

  • Intermolecular Paramagnetic Relaxation Enhancement (PRE) Studies of Transient Complexes in Intrinsically Disordered Proteins

    Pages 45-53

    Janowska, Maria K. (et al.)

  • Detection of Helical Intermediates During Amyloid Formation by Intrinsically Disordered Polypeptides and Proteins

    Pages 55-66

    Abedini, Andisheh (et al.)

  • Fluorescence Correlation Spectroscopy: A Tool to Study Protein Oligomerization and Aggregation In Vitro and In Vivo

    Pages 67-87

    Sahoo, Bankanidhi (et al.)

Buy this book

eBook $109.00
price for USA in USD
  • ISBN 978-1-4939-2978-8
  • Digitally watermarked, DRM-free
  • Included format: PDF, EPUB
  • ebooks can be used on all reading devices
  • Immediate eBook download after purchase
Hardcover $169.99
price for USA in USD
  • ISBN 978-1-4939-2977-1
  • Free shipping for individuals worldwide
  • Institutional customers should get in touch with their account manager
  • Covid-19 shipping restrictions
  • Usually ready to be dispatched within 3 to 5 business days, if in stock
Softcover $139.99
price for USA in USD
  • ISBN 978-1-4939-5005-8
  • Free shipping for individuals worldwide
  • Institutional customers should get in touch with their account manager
  • Covid-19 shipping restrictions
  • Usually ready to be dispatched within 3 to 5 business days, if in stock
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Bibliographic Information

Bibliographic Information
Book Title
Protein Amyloid Aggregation
Book Subtitle
Methods and Protocols
Editors
  • David Eliezer
Series Title
Methods in Molecular Biology
Series Volume
1345
Copyright
2016
Publisher
Humana Press
Copyright Holder
Springer Science+Business Media New York
eBook ISBN
978-1-4939-2978-8
DOI
10.1007/978-1-4939-2978-8
Hardcover ISBN
978-1-4939-2977-1
Softcover ISBN
978-1-4939-5005-8
Series ISSN
1064-3745
Edition Number
1
Number of Pages
XIV, 314
Number of Illustrations
24 b/w illustrations, 49 illustrations in colour
Topics