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Default Deuterium spin relaxation of fractionally deuterated ribonuclease H using paired 475 and 950 MHz NMR spectrometers

Deuterium spin relaxation of fractionally deuterated ribonuclease H using paired 475 and 950 MHz NMR spectrometers

Deuterium (²H) spin relaxation of ^(13)CH(2)D methyl groups has been widely applied to investigate picosecond-to-nanosecond conformational dynamics in proteins by solution-state NMR spectroscopy. The B(0) dependence of the ²H spin relaxation rates is represented by a linear relationship between the spectral density function at three discrete frequencies J(0), J(?(D)) and J(2?(D)). In this study, the linear relation between ²H relaxation rates at B(0) fields separated by a factor of two and the...

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