Probing slow protein dynamics by adiabatic R and R NMR experiments

Silvia Mangia, Nathaniel J. Traaseth, Gianluigi Veglia, Michael Garwood, Shalom Michaeli

Research output: Contribution to journalArticlepeer-review


Slow μs/ms dynamics involved in protein folding, binding, catalysis, and allostery are currently detected using NMR dispersion experiments such as CPMG (Carr-Purcell-Meiboom-Gill) or spin-lock R . In these methods, protein dynamics are obtained by analyzing relaxation dispersion curves obtained from either changing the time spacing between 180° pulses or by changing the effective spin-locking field strength. In this Communication, we introduce a new method to induce a dispersion of relaxation rates. Our approach relies on altering the shape of the adiabatic full passage pulse and is conceptually different from existing approaches. By changing the nature of the adiabatic radiofrequency irradiation, we are able to obtain rotating frame R and R dispersion curves that are sensitive to slow μs/ms protein dynamics (demonstrated with ubiquitin). The strengths of this method are to (a) extend the dynamic range of the relaxation dispersion analysis, (b) avoid the need for multiple magnetic field strengths to extract dynamic parameters, (c) measure accurate relaxation rates that are independent of frequency offset, and (d) reduce the stress to NMR hardware (e.g., cryoprobes).

Original languageEnglish (US)
Pages (from-to)9979-9981
Number of pages3
JournalJournal of the American Chemical Society
Issue number29
StatePublished - Jul 28 2010

ASJC Scopus subject areas

  • Catalysis
  • General Chemistry
  • Biochemistry
  • Colloid and Surface Chemistry


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