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Intrinsically Disordered Protein Analysis

Volume 1, Methods and Experimental Tools

  • Book
  • © 2012

Overview

Editors:
  1. Vladimir N. Uversky

    1. Department of Molecular Medicine, College of Medicine, University of South Florida, Tampa, USA

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    You can also search for this editor in PubMed   Google Scholar

  2. A. Keith Dunker

    1. Dept. Biochemistry & Molecular Biology, Center for Computational Biology &, Indiana University, Indianapolis, USA

    View editor publications

    You can also search for this editor in PubMed   Google Scholar

  • Details experimental methods used to identify IDP's and to analyze their stucture
  • Provides step-by-step detail essential for reproducible results
  • Contains key notes and implementation advice from the experts
  • Includes supplementary material: sn.pub/extras

Part of the book series: Methods in Molecular Biology (MIMB, volume 895)

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Table of contents (29 protocols)

  1. Front Matter

    Pages i-xiv
    Download chapter PDF

  2. Assessing IDPS in the Living Cell

    1. Front Matter

      Pages 1-1
      Download chapter PDF

    2. Determination of IUP Based on Susceptibility for Degradation by Default

      • Peter Tsvetkov, Yosef Shaul
      Pages 3-18

    3. In-Cell NMR of Intrinsically Disordered Proteins in Prokaryotic Cells

      • Yutaka Ito, Tsutomu Mikawa, Brian O. Smith
      Pages 19-31

    4. In-Cell NMR in Xenopus laevis Oocytes

      • Rossukon Thongwichian, Philipp Selenko
      Pages 33-41

    5. In-Cell NMR in Mammalian Cells: Part 1

      • Beata Bekei, Honor May Rose, Michaela Herzig, Alexander Dose, Dirk Schwarzer, Philipp Selenko
      Pages 43-54

    6. In-Cell NMR in Mammalian Cells: Part 2

      • Beata Bekei, Honor May Rose, Michaela Herzig, Philipp Selenko
      Pages 55-66

    7. In-Cell NMR in Mammalian Cells: Part 3

      • Beata Bekei, Honor May Rose, Michaela Herzig, Heike Stephanowitz, Eberhard Krause, Philipp Selenko
      Pages 67-83

    8. Fourier Transform Infrared Microspectroscopy of Complex Biological Systems: From Intact Cells to Whole Organisms

      • Diletta Ami, Antonino Natalello, Silvia Maria Doglia
      Pages 85-100

    9. Studying IDP Stability and Dynamics by Fast Relaxation Imaging in Living Cells

      • Apratim Dhar, Maxim Prigozhin, Hannah Gelman, Martin Gruebele
      Pages 101-111

  3. NMR-Based Techniques

    1. Front Matter

      Pages 113-113
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    2. Measurement and Analysis of NMR Residual Dipolar Couplings for the Study of Intrinsically Disordered Proteins

      • Loïc Salmon, Malene Ringkjøbing Jensen, Pau Bernadó, Martin Blackledge
      Pages 115-125

    3. Distance Information for Disordered Proteins from NMR and ESR Measurements Using Paramagnetic Spin Labels

      • David Eliezer
      Pages 127-138

    4. Using Chemical Shifts to Assess Transient Secondary Structure and Generate Ensemble Structures of Intrinsically Disordered Proteins

      • Stepan Kashtanov, Wade Borcherds, Hongwei Wu, Gary W. Daughdrill, F. Marty Ytreberg
      Pages 139-152

    5. Magic Angle Spinning Solid-State NMR Experiments for Structural Characterization of Proteins

      • Lichi Shi, Vladimir Ladizhansky
      Pages 153-165

    6. Wide-Line NMR and Protein Hydration

      • K. Tompa, M. Bokor, P. Tompa
      Pages 167-196

    7. 5-Fluoro-d,l-Tryptophan as a Dual NMR and Fluorescent Probe of α-Synuclein

      • Candace M. Pfefferkorn, Jennifer C. Lee
      Pages 197-209

    8. Alpha Proton Detection Based Backbone Assignment of Intrinsically Disordered Proteins

      • Perttu Permi, Maarit Hellman
      Pages 211-226

  4. Vibrational Spectroscopy

    1. Front Matter

      Pages 227-227
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    2. Fourier Transform Infrared Spectroscopy of Intrinsically Disordered Proteins: Measurement Procedures and Data Analyses

      • Antonino Natalello, Diletta Ami, Silvia Maria Doglia
      Pages 229-244
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Keywords

About this book

Over the past decade, there has been an explosive development of research of intrinsically disordered proteins (IDPs), which are also known as unfolded proteins. Structural biologists now recognize that the functional diversity provided by disordered regions complements the functional repertoire of ordered protein regions. In Intrinsically Disordered Protein Analysis :Methods and Experimental Tools, expert researchers explore the high abundance of IDPs in various organisms, their unique structural features, numerous functions, and crucial associations with different diseases. Volume 1 includes sections on assessing IDPs in the living cell,NMR based techniques, vibrational spectroscopy, and other spectroscopic techniques. Written in the highly successful Methods in Molecular Biologyâ„¢ series format, the chapters include the kind of detailed description and implementation advice that is crucial for getting optimal results in the laboratory.

 

Thorough and intuitive, Intrinsically Disordered Protein Analysis: Methods and Experimental Tools helps scientists further their investigations of these fascinating and dynamic molecules.

 

Editors and Affiliations

  • Department of Molecular Medicine, College of Medicine, University of South Florida, Tampa, USA

    Vladimir N. Uversky

  • Dept. Biochemistry & Molecular Biology, Center for Computational Biology &, Indiana University, Indianapolis, USA

    A. Keith Dunker

Bibliographic Information

  • Book Title: Intrinsically Disordered Protein Analysis

  • Book Subtitle: Volume 1, Methods and Experimental Tools

  • Editors: Vladimir N. Uversky, A. Keith Dunker

  • Series Title: Methods in Molecular Biology

  • DOI: https://doi.org/10.1007/978-1-61779-927-3

  • Publisher: Humana Totowa, NJ

  • eBook Packages: Springer Protocols

  • Copyright Information: Springer Science+Business Media, LLC 2012

  • Hardcover ISBN: 978-1-61779-926-6Published: 05 July 2012

  • Softcover ISBN: 978-1-4939-6230-3Published: 23 August 2016

  • eBook ISBN: 978-1-61779-927-3Published: 04 July 2012

  • Series ISSN: 1064-3745

  • Series E-ISSN: 1940-6029

  • Edition Number: 1

  • Number of Pages: XIV, 511

  • Topics: Protein Science, Protein Structure

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