Journal
JOURNAL OF BIOMOLECULAR NMR
Volume 37, Issue 2, Pages 147-157Publisher
SPRINGER
DOI: 10.1007/s10858-006-9125-7
Keywords
cross-relaxation; cross-correlation; protein; dynamics; relaxation; NMR
Categories
Ask authors/readers for more resources
The heteronuclear N-15-{H-1} NOE values are typically determined by taking the ratio of N-15 signal intensities recorded in the presence and absence of H-1 saturation prior to evolution of N-15 magnetization. Since the intensity ratio of two independent experiments is taken, complete recovery of N-15 magnetization during the scan repetition delay is critical to obtain reliable NOE values. Because it may not be practical to wait for the complete recovery of magnetization at high magnetic fields, Solomon equations may be used to correct measured NOE values. Here, based on experiments and simulations, we show that since the cross-correlation between H-1-N-15 dipole and N-15 chemical shift anisotropy becomes significant at high fields for small or deuterated proteins, measured NOE values can not be accurately corrected based on the Solomon equations. We also discuss ranges of rotational correlation times and proton spin-flip rate, in which the NOE values can be corrected by the equations.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available