To investigate the backbone dynamics of roteins I5N longitudinal and transverse relaxation experiments combined with (lH, r5N] NOE measurements together with molecular dynamics simulations were carried out using ribonuclease TI and the complex of ribonuclease TI with 2'GMP as a model protein. The in
Solution of the spatial structure of dimeric transmembrane domains of proteins by heteronuclear NMR spectroscopy and molecular modeling
โ Scribed by Volynsky, P. E. ;Bocharov, E. V. ;Nolde, D. E. ;Vereschaga, Ya. A. ;Mayzel, M. L. ;Mineev, K. S. ;Mineeva, E. A. ;Pustovalova, Yu. E. ;Gagnidze, I. A. ;Efremov, R. G. ;Arseniev, A. S.
- Book ID
- 110156827
- Publisher
- Biophysical Society of Japan
- Year
- 2006
- Tongue
- English
- Weight
- 309 KB
- Volume
- 51
- Category
- Article
- ISSN
- 1349-2942
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
## Abstract The structure and dynamics of the ureaโdenatured B1 immunoglobulin binding domain of streptococcal protein G (GB1) has been investigated by multidimensional heteronuclear NMR spectroscopy. Complete ^1^H, ^15^N, and ^13^C assignments are obtained by means of sequential throughโbond corre
The growth factor receptor-bound protein-2 (Grb2) is an adaptor protein that mediates signal transduction pathways. Chemical shift assignments were obtained for the SH2 domain of Grb2 by heteronuclear NMR spectroscopy, employing the uniformly 13C-/15N-enriched protein as well as the protein containi
pSRII, pH 5.9, 60 mm DHPC (non-deuterated). Maximum entropy data reconstruction was used in F2 and F3. 15 N relaxation data were measured at 14.1 T on a 2 H, 15 N-labeled sample using TROSYmodified sequences. 3D 15 N NOESY experiments were recorded as HMQC and TROSY versions.