Intrinsically Disordered Proteins Studied by NMR Spectroscopy

  • Isabella C. Felli
  • Roberta Pierattelli

Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 870)

Table of contents

  1. Front Matter
    Pages i-xiii
  2. Biao Fu, Michele Vendruscolo
    Pages 35-48
  3. Bernhard Brutscher, Isabella C. Felli, Sergio Gil-Caballero, Tomáš Hošek, Rainer Kümmerle, Alessandro Piai et al.
    Pages 49-122
  4. Jaka Kragelj, Martin Blackledge, Malene Ringkjøbing Jensen
    Pages 123-147
  5. Dennis Kurzbach, Georg Kontaxis, Nicolas Coudevylle, Robert Konrat
    Pages 149-185
  6. Eduardo O. Calçada, Magdalena Korsak, Tatiana Kozyreva
    Pages 187-213
  7. Michael Kachala, Erica Valentini, Dmitri I. Svergun
    Pages 261-289
  8. Pallab Bhowmick, Mainak Guharoy, Peter Tompa
    Pages 291-318
  9. Cesyen Cedeño, Hadas Raveh-Hamit, András Dinnyés, Peter Tompa
    Pages 319-334
  10. Mihaly Varadi, Peter Tompa
    Pages 335-349
  11. Jenny Erales, David Blocquel, Johnny Habchi, Matilde Beltrandi, Antoine Gruet, Marion Dosnon et al.
    Pages 351-381
  12. Priyanka Joshi, Michele Vendruscolo
    Pages 383-400

About this book


This book discusses the paradigm-shifting phenomenon of intrinsically disordered proteins (IDPs) and hybrid proteins containing ordered domains and functional IDP regions (IDPRs). The properties of IDPs and IDPRs are highly complementary to those deriving from the presence of a unique and well-defined three-dimensional fold. Ignored for a long time in high-resolution studies of proteins, intrinsic protein disorder is now recognized as one of the key features for a large variety of cellular functions, where structural flexibility presents a functional advantage in terms of binding plasticity and promiscuity and this volume explores this exciting new research.

Recent progress in the field has radically changed our perspective to study IDPs through NMR: increasingly complex IDPs can now be characterized, a wide range of observables can be determined reporting on the structural and dynamic properties, computational methods to describe the structure and dynamics are in continuous development and IDPs can be studied in environments as complex as whole cells. This volume communicates the new exciting possibilities offered by NMR and presents open questions to foster further developments.

Intrinsically Disordered Proteins Studied by NMR Spectroscopy provides a snapshot to researchers entering the field as well as providing a current overview for more experienced scientists in related areas.


NMR spectroscopy bioinformatics functional IDP regions intrinsically disordered proteins nuclear magnetic resonance structural properties

Editors and affiliations

  • Isabella C. Felli
    • 1
  • Roberta Pierattelli
    • 2
  1. 1.CERM and Department of Chemistry"Ugo Schiff" University of FlorenceFlorenceItaly
  2. 2.CERM and Department of Chemistry"Ugo Schiff" University of FlorenceFlorenceItaly

Bibliographic information