Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 131, Issue 17, Pages 6048-+Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja809526q
Keywords
-
Categories
Funding
- NSF [MCB-0347100, 0843141]
- NIH [GM 47021, 5G12 RR06030]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0843141] Funding Source: National Science Foundation
Ask authors/readers for more resources
The steady-state {H-1}-N-15 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 N-15 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.
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