2022 - Research.com Chemistry in Canada Leader Award
2020 - Member of the National Academy of Sciences
2019 - Nakanishi Prize, Chemical Society of Japan and the American Chemical Society.
2017 - Canada Gairdner International Award
2010 - Fellow of the Royal Society, United Kingdom
2006 - Fellow of the Royal Society of Canada Academy of Science
1995 - Fellow of Alfred P. Sloan Foundation
Lewis E. Kay mainly focuses on Nuclear magnetic resonance spectroscopy, Crystallography, Protein structure, Nuclear magnetic resonance and Analytical chemistry. His study on Nuclear magnetic resonance spectroscopy also encompasses disciplines like
His Protein structure research incorporates themes from Biophysics, Stereochemistry and Protein folding. Lewis E. Kay has included themes like Resolution and NMR spectra database in his Nuclear magnetic resonance study. His Analytical chemistry research is multidisciplinary, relying on both Triple-resonance nuclear magnetic resonance spectroscopy, Pulse sequence, Carbon-13, Chemical exchange and Proton.
Lewis E. Kay focuses on Nuclear magnetic resonance spectroscopy, Crystallography, Relaxation, Analytical chemistry and Biophysics. Lewis E. Kay combines subjects such as Protein structure, Molecule, Chemical physics and Chemical shift with his study of Nuclear magnetic resonance spectroscopy. His Crystallography research is multidisciplinary, incorporating elements of SH3 domain, Two-dimensional nuclear magnetic resonance spectroscopy, Kinetics and Protein folding.
His Relaxation study also includes fields such as
Lewis E. Kay focuses on Biophysics, Nuclear magnetic resonance spectroscopy, Chemical physics, Conformational isomerism and Biochemistry. His Biophysics research incorporates elements of Protease, Chaperone, Protein folding, Thermoplasma acidophilum and Allosteric regulation. His Nuclear magnetic resonance spectroscopy study combines topics in areas such as Protein structure, Molecule, Protein aggregation and Molecular machine.
His research in Chemical physics intersects with topics in Millisecond, Relaxation, Solvent, Molecular dynamics and Crystallography. His Relaxation study contributes to a more complete understanding of Nuclear magnetic resonance. The Conformational isomerism study combines topics in areas such as Biomolecule, Folding, Analytical chemistry, Chemical exchange and Chemical shift.
His primary areas of investigation include Biophysics, Conformational isomerism, Nuclear magnetic resonance spectroscopy, Biochemistry and Protein folding. His research in Conformational isomerism intersects with topics in SH3 domain, Biomolecule, Excited state, Analytical chemistry and Protein structure. His biological study spans a wide range of topics, including Folding, Crystallography, Molecule and Chemical physics.
The concepts of his Crystallography study are interwoven with issues in Protein dynamics and Kinetics. His work deals with themes such as Proteome, Relaxation and Molecular dynamics, which intersect with Molecule. Lewis E. Kay focuses mostly in the field of Protein folding, narrowing it down to matters related to Energy landscape and, in some cases, Native state.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
Backbone Dynamics of a Free and a Phosphopeptide-Complexed Src Homology 2 Domain Studied by 15N NMR Relaxation
Neil A. Farrow;Ranjith Muhandiram;Alex U. Singer;Steven M. Pascal.
Biochemistry (1994)
Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease.
Lewis E. Kay;Dennis A. Torchia;Ad Bax.
Biochemistry (1989)
Three-dimensional triple-resonance NMR Spectroscopy of isotopically enriched proteins
Lewis E Kay;Mitsuhiko Ikura;Rolf Tschudin;Ad Bax.
Journal of Magnetic Resonance (1990)
Intrinsic dynamics of an enzyme underlies catalysis
Elan Z. Eisenmesser;Oscar Millet;Wladimir Labeikovsky;Dmitry M. Korzhnev.
Nature (2005)
A novel approach for sequential assignment of proton, carbon-13, and nitrogen-15 spectra of larger proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin
Mitsuhiko Ikura;Lewis E. Kay;Ad Bax.
Biochemistry (1990)
Overcoming the overlap problem in the assignment of proton NMR spectra of larger proteins by use of three-dimensional heteronuclear proton-nitrogen-15 Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: application to interleukin 1.beta.
Dominique Marion;Paul C. Driscoll;Lewis E. Kay;Paul T. Wingfield.
Biochemistry (1989)
Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins
G. Marius Clore;Attila Szabo;Ad Bax;Lewis E. Kay.
Journal of the American Chemical Society (1990)
Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible.
Gaetano Barbato;Mitsuhiko Ikura;Lewis E. Kay;Richard W. Pastor.
Biochemistry (1992)
Gradient-Enhanced Triple-Resonance Three-Dimensional NMR Experiments with Improved Sensitivity
D.R. Muhandiram;L.E. Kay.
Journal of Magnetic Resonance, Series B (1994)
New Tools Provide New Insights in NMR Studies of Protein Dynamics
Anthony Mittermaier;Lewis E. Kay.
Science (2006)
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