Accurate sampling of high-frequency motions in proteins by steady-state 15N-{ 1H} nuclear overhauser effect measurements in the presence of cross-correlated relaxation

Fabien Ferrage, David Cowburn, Ranajeet Ghose

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49 Citations (Scopus)

Abstract

The steady-state { 1H}- 15N NOE experiment is used in most common NMR analyses of backbone dynamics to accurately ascertain the effects of the fast dynamic modes. We demonstrate here that, in its most common implementation, this experiment generates an incorrect steady state in the presence of CSA/dipole cross-correlated relaxation leading to large errors in the characterization of these high-frequency modes. This affects both the quantitative and qualitative interpretation of 15N backbone relaxation in dynamic terms. We demonstrate further that minor changes in the experimental implementation effectively remove these errors and allow a more accurate interpretation of protein backbone dynamics.

Original languageEnglish (US)
Pages (from-to)6048-6049
Number of pages2
JournalJournal of the American Chemical Society
Volume131
Issue number17
DOIs
StatePublished - May 6 2009

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Sampling
Proteins
Experiments
Nuclear magnetic resonance

ASJC Scopus subject areas

  • Chemistry(all)
  • Catalysis
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

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AU - Ghose, Ranajeet

PY - 2009/5/6

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N2 - The steady-state { 1H}- 15N NOE experiment is used in most common NMR analyses of backbone dynamics to accurately ascertain the effects of the fast dynamic modes. We demonstrate here that, in its most common implementation, this experiment generates an incorrect steady state in the presence of CSA/dipole cross-correlated relaxation leading to large errors in the characterization of these high-frequency modes. This affects both the quantitative and qualitative interpretation of 15N backbone relaxation in dynamic terms. We demonstrate further that minor changes in the experimental implementation effectively remove these errors and allow a more accurate interpretation of protein backbone dynamics.

AB - The steady-state { 1H}- 15N NOE experiment is used in most common NMR analyses of backbone dynamics to accurately ascertain the effects of the fast dynamic modes. We demonstrate here that, in its most common implementation, this experiment generates an incorrect steady state in the presence of CSA/dipole cross-correlated relaxation leading to large errors in the characterization of these high-frequency modes. This affects both the quantitative and qualitative interpretation of 15N backbone relaxation in dynamic terms. We demonstrate further that minor changes in the experimental implementation effectively remove these errors and allow a more accurate interpretation of protein backbone dynamics.

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