A structural mode-coupling approach to N-15 NMR relaxation in proteins

Citation
V. Tugarinov et al., A structural mode-coupling approach to N-15 NMR relaxation in proteins, J AM CHEM S, 123(13), 2001, pp. 3055-3063
Citations number
35
Categorie Soggetti
Chemistry & Analysis",Chemistry
Journal title
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
ISSN journal
00027863 → ACNP
Volume
123
Issue
13
Year of publication
2001
Pages
3055 - 3063
Database
ISI
SICI code
0002-7863(20010404)123:13<3055:ASMATN>2.0.ZU;2-5
Abstract
The two-body Slowly Relaxing Local Structure (SRLS) model was applied to N- 15 NMR spin relaxation in proteins and compared with the commonly used orig inal and extended model-free (IMF) approaches. In MF, the dynamic modes are assumed to be decoupled, local ordering at the N-H sites is represented by generalized order parameters, and internal motions are described by effect ive correlation times. SRLS accounts for dynamical coupling between the glo bal diffusion of the protein and the internal motion of the N-H bond vector . The local ordering associated with the coupling potential and the interna l N-H diffusion are tensors with orientations that may be tilted relative t o the global diffusion and magnetic frames. SRLS generates spectral density functions that differ from the MF formulas. The MF spectral densities can be regarded as limiting cases of the SRLS spectral density. SRLS-based mode l-fitting and model-selection schemes similar to the currently used MF-base d ones were devised, and a correspondence between analogous SRLS and model- free parameters was established. It was found that experimental NMR data ar e sensitive to the presence of mixed modes. Our results showed that MF can significantly overestimate order parameters and underestimate local motion correlation times in proteins. The extent of these digressions in the deriv ed microdynamic parameters is estimated in the various parameter ranges, an d correlated with the time scale separation between local and global motion s. The SRLS-based analysis was tested extensively on N-15 relaxation data f rom several isotropically tumbling proteins. The results of SRLS-based fitt ing are illustrated with RNase H from E. coli, a protein extensively studie d previously with MF.