Heteronuclear Adiabatic Relaxation Dispersion (HARD) for quantitative analysis of conformational dynamics in proteins.

Abstract

NMR relaxation methods probe biomolecular motions over a wide range of timescales. In particular, the rotating frame spin-lock R(1ρ) and Carr-Purcell-Meiboom-Gill (CPMG) R(2) experiments are commonly used to characterize μs to ms dynamics, which play a critical role in enzyme folding and catalysis. In an effort to complement these approaches, we introduced… (More)
DOI: 10.1016/j.jmr.2012.03.024

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Cite this paper

@article{Traaseth2012HeteronuclearAR, title={Heteronuclear Adiabatic Relaxation Dispersion (HARD) for quantitative analysis of conformational dynamics in proteins.}, author={Nathaniel J. Traaseth and Fa-An Chao and Larry R. Masterson and Silvia Mangia and Michael Garwood and Shalom Michaeli and Burckhard Seelig and Gianluigi Veglia}, journal={Journal of magnetic resonance}, year={2012}, volume={219}, pages={75-82} }