Observation of heteronuclear overhauser effects confirms the 15N-1H dipolar relaxation mechanism in a crystalline protein.
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.
Giraud
Nicolas
N
Laboratoire de Chimie (UMR 5182 CNRS/ENS), Ecole Normale Supérieure de Lyon, 69364 Lyon, France.
Sein
Julien
J
Pintacuda
Guido
G
Böckmann
Anja
A
Lesage
Anne
A
Blackledge
Martin
M
Emsley
Lyndon
L
D001426:Bacterial Proteins / Q000737:chemistry*; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010750:Phosphoproteins / Q000737:chemistry*; D011522:Protons
D001426:Bacterial Proteins; C118042:Crh protein, Bacillus subtilis; D009587:Nitrogen Isotopes; D010750:Phosphoproteins; D011522:Protons