DOI

  • Dmitry M. Korzhnev
  • Nikolai R. Skrynnikov
  • Oscar Millet
  • Dennis A. Torchia
  • Lewis E. Kay

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 оригиналаанглийский
Страницы (с-по)10743-10753
Число страниц11
ЖурналJournal of the American Chemical Society
Том124
Номер выпуска36
DOI
СостояниеОпубликовано - 11 сен 2002

    Предметные области Scopus

  • Катализ
  • Химия (все)
  • Биохимия
  • Коллоидная химия и химия поверхности

ID: 74229346