Atomic resolution conformational dynamics of intrinsically disordered proteins from NMR spin relaxation

Prog Nucl Magn Reson Spectrosc. 2017 Nov;102-103:43-60. doi: 10.1016/j.pnmrs.2017.06.001. Epub 2017 Jul 10.


Nuclear magnetic resonance (NMR) spectroscopy is one of the most powerful experimental approaches for investigating the conformational behaviour of intrinsically disordered proteins (IDPs). IDPs represent a significant fraction of all proteomes, and, despite their importance for understanding fundamental biological processes, the molecular basis of their activity still remains largely unknown. The functional mechanisms exploited by IDPs in their interactions with other biomolecules are defined by their intrinsic dynamic modes and associated timescales, justifying the considerable interest over recent years in the development of technologies adapted to measure and describe this behaviour. NMR spin relaxation delivers information-rich, site-specific data reporting on conformational fluctuations occurring throughout the molecule. Here we review recent progress in the use of 15N relaxation to identify local backbone dynamics and long-range chain-like motions in unfolded proteins.

Keywords: Activation energy; Arrhenius relationship; Intrinsically disordered protein; Nuclear magnetic resonance; Protein dynamics; Segmental motion; Spin relaxation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Intrinsically Disordered Proteins / chemistry*
  • Kinetics
  • Magnetic Resonance Spectroscopy / methods*
  • Models, Molecular
  • Protein Conformation
  • Proteome / chemistry
  • Thermodynamics


  • Intrinsically Disordered Proteins
  • Proteome