Simultaneous quantification of protein order and disorder using NMR spectroscopy - Archive ouverte HAL
Journal Articles Nature Chemical Biology Year : 2017

Simultaneous quantification of protein order and disorder using NMR spectroscopy

Pietro Sormanni
  • Function : Author
Damiano Piovesan
Gabriella T Heller
  • Function : Author
Massimiliano Bonomi
Predrag Kukic
  • Function : Author
Carlo Camilloni
  • Function : Author
Monika Fuxreiter
  • Function : Author
Zsuzsanna Dosztanyi
  • Function : Author
Rohit Pappu
M Madan Babu
  • Function : Author
Sonia Longhi
Peter Tompa
A Keith Dunker
  • Function : Author
Vladimir N Uversky
Silvio C E Tosatto
  • Function : Author
Michele Vendruscolo
  • Function : Author

Abstract

Nuclear magnetic resonance spectroscopy is transforming our view of proteins by revealing how their structures and dynamics are closely intertwined to underlie their functions and interactions. Effective descriptions of protein dynamics are uncovering the presence and biological relevance of highly heterogeneous conformational states of proteins, which go beyond the traditional dichotomy between order and disorder by spanning the continuum between them.
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Dates and versions

hal-03153894 , version 1 (26-02-2021)

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Pietro Sormanni, Damiano Piovesan, Gabriella T Heller, Massimiliano Bonomi, Predrag Kukic, et al.. Simultaneous quantification of protein order and disorder using NMR spectroscopy. Nature Chemical Biology, 2017, ⟨10.1038/nchembio.2331⟩. ⟨hal-03153894⟩
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