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Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease.
The use of novel two-dimensional nuclear magnetic resonance (NMR) pulse sequences to provide insight into protein dynamics is described, suggesting that there is no correlation between these rapid small amplitude motions and secondary structure for S. Nase. Expand
Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation.
Overall, higher order parameters were not found in the peptide-bound form, indicating that on average, picosecond-time-scale disorder is not reduced upon binding peptide, and the relaxation data of the SH2-phosphopeptide complex were fit with fewer exchange terms than the uncomplexed form. Expand
Gradient-Enhanced Triple-Resonance Three-Dimensional NMR Experiments with Improved Sensitivity
Abstract The sensitivities of a number of gradient and nongradient versions of triple-resonance experiments are compared by quantitating the signal-to-noise ratios in spectra recorded on Cellulomonas… Expand
Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques
- O. Zhang, L. Kay, J. P. Olivier, J. Forman-Kay
- Chemistry, Medicine
- Journal of biomolecular NMR
- 1 November 1994
NMR methods which exploit the chemical shift dispersion of the 15N resonances of unfolded states and pulsed field gradient water suppression approaches for avoiding saturation and dephasing of amide protons which rapidly exchange with solvent were utilized for the assignment. Expand
Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible.
The backbone dynamics of Ca(2+)-saturated recombinant Drosophila calmodulin has been studied by 15N longitudinal and transverse relaxation experiments, combined with 15N(1H) NOE measurements, showing a high degree of mobility near the middle of the central helix and anisotropy observed in the motion of the two globular cal modulin domains is much smaller than expected. Expand
Methods for Measurement of Intermolecular NOEs by Multinuclear NMR Spectroscopy: Application to a Bacteriophage λ N-Peptide/boxB RNA Complex
New pulse schemes for recording intermolecular NOEs in a molecular complex consisting of 15N,13C labeled and unlabeled components are presented. The pulse sequences select for magnetization… Expand
Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins
α Helix-RNA Major Groove Recognition in an HIV-1 Rev Peptide-RRE RNA Complex
The solution structure of a human immunodeficiency virus type-1 (HIV-1) Rev peptide bound to stem-loop IIB of the Rev response element (RRE) RNA was solved by nuclear magnetic resonance spectroscopy.… Expand
Three-dimensional triple-resonance NMR Spectroscopy of isotopically enriched proteins. 1990.
The principles of these triple-resonance experiments are described in terms of the operator formalism and special attention is paid to removal of undesired J splittings in the 3D spectra. Expand
Latent and active p53 are identical in conformation
- A. Ayed, F. Mulder, G. Yi, Y. Lu, L. Kay, C. Arrowsmith
- Biology, Medicine
- Nature Structural Biology
- 1 September 2001
It is shown on the basis of chemical shifts that dimeric p53 both containing and lacking the C-terminal domain are identical in conformation and that theC-terminus does not interact with other p53 domains, ruling out an allosteric model for the regulation of p53. Expand