Cross-correlation suppressed T1 and NOE experiments for protein side-chain 13CH2 groups |
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Authors: | Jin Changwen Prompers Jeanine J Brüschweiler Rafael |
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Affiliation: | (1) Beijing NMR Center, Peking University, Beijing, China;(2) Carlson School of Chemistry and Biochemistry, Clark University, Worcester, MA, 01610, U.S.A. |
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Abstract: | Relaxation measurements of side-chain 13CH2-groups of uniformly 13C labeled human ubiquitin were performed at 600 MHz and 800 MHz magnetic field strength at 30°C. Dipole-dipole cross-correlated relaxation effects in T1 experiments were suppressed by the combination of radio-frequency pulses and pulsed field gradients during the relaxation delay leading to monoexponential relaxation decays that allow a more accurate extraction of the 13C T1 relaxation times. Heteronuclear 1H-13C NOEs obtained by using different proton saturation schemes indicate that the influence of cross-correlation is small. The experimental T1 and NOE data were interpreted in a model-free way in terms of a generalized order parameter and an internal correlation time. |
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Keywords: | methylene groups NMR relaxation NOE protein side-chain dynamics suppression of cross-correlated relaxation T1 |
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