Observation of heteronuclear overhauser effects confirms the 15N-1H dipolar relaxation mechanism in a crystalline protein

J Am Chem Soc. 2006 Sep 27;128(38):12398-9. doi: 10.1021/ja064037g.

Abstract

The observation of proton to nitrogen-15 heteronuclear Overhauser effects in the microcrystalline protein Crh is used to confirm that the principal mechanism of relaxation of amide nitrogens is due to the fluctuation of the N-H dipolar couplings caused by N-H bond dynamics. Our observations reveal the central role of water as the main source of proton magnetization, and we provide an analysis of the different pathways that could lead to the observed results.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Nitrogen Isotopes
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Phosphoproteins / chemistry*
  • Protons

Substances

  • Bacterial Proteins
  • Crh protein, Bacillus subtilis
  • Nitrogen Isotopes
  • Phosphoproteins
  • Protons