Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
Rotating-frame relaxation rates, R1p, are often measured in NMR studies of protein dynamics. We show here that large systematic errors can be introduced into measured values of heteronuclear R1p rates using schemes which are usually employed to suppress cross-correlation between dipole-dipole and CSA relaxation mechanisms. For example, in a scalar-coupled two-spin X-H spin system the use of 1H WALTZ16 decoupling or 1H pulses applied at regularly spaced intervals leads to a significant overestimation of heteronuclear R1p values. The problem is studied experimentally and theoretically for 15N-1H and 13C-1H spin pairs, and simple schemes are described which eliminate the artifacts. The approaches suggested are essential replacements of existing methodology if accurate dynamics parameters are to be extracted from spin-lock relaxation data sets.
Язык оригинала | английский |
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Страницы (с-по) | 10743-10753 |
Число страниц | 11 |
Журнал | Journal of the American Chemical Society |
Том | 124 |
Номер выпуска | 36 |
DOI | |
Состояние | Опубликовано - 11 сен 2002 |
ID: 74229346