Observation and Relaxation Properties of Individual Fast-Relaxing Proton Transitions in [CH3]-Methyl-Labeled, Deuterated Proteins
Observation and Relaxation Properties of Individual Fast-Relaxing Proton Transitions in [CH3]-Methyl-Labeled, Deuterated Proteins
Publication year: 2012 Source: Journal of Magnetic Resonance, Available online 2 March 2012</br> Hechao*Sun, Vitali*Tugarinov</br> A pair of NMR experiments is developed for separation of individual fast-relaxing transitions inCH3methyl groups of methyl-protonated, highly deuterated proteins, and the measurement of their relaxation rates. Intra-methylH-H/H-C dipole-dipole cross-correlated spin relaxation that differentiates the rates of the fast-relaxing transitions depending on the state ofC spins, is measured in the selectively [CH3]-methyl-labeled, deuterated ubiquitin at 10, 27, and 40 °C. In contrast with previous observations, theH-H/H-C cross-correlated relaxation rates measured from relaxation rates of single-quantum proton transitions serve as good measures of side-chain order even in proteins with global rotational correlation times significantly less than 10 ns.</br> Graphical abstract http://www.sciencedirect.com/cache/M...000742-fx1.sml</br>Highlights ? Experiments are presented for separation of individualH transitions in methyls. ? Intra-methylH-H/H-C cross-correlations in these transitions are quantified.H-H/H-C cross-correlations serve as good measures of side-chain ordering.</br></br> Source: Journal of Magnetic Resonance |
All times are GMT. The time now is 11:53 AM. |
Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2024, Jelsoft Enterprises Ltd.
Search Engine Friendly URLs by vBSEO 3.6.0
Copyright, BioNMR.com, 2003-2013