| Citation | Professor Lewis Edward Kay, Professor of Biochemistry, Molecular Genetics and Chemistry, Departments of Biochemistry, Molecular Genetics and Chemistry, University of Toronto
NMR has made a major impact in the study of the structures and properties of biomolecules. Lewis Kay and his group at the University of Toronto have developed many of the recent technical advances that have pushed the size limit of protein complexes that can be examined by NMR spectroscopy beyond 500 kDa. For example, methyl-TROSY has been used by the Kay group to elucidate the structure and aspects of the dynamics of the 670 kDa 20S proteosome core particle. In addition, Kay and his group have delineated the detailed consequences of the binding of ligands to proteins; in the case of aspartate transcarbamoylase, for example, they have defined the nature of the allostery associated with the binding of nucleotide effector molecules. Professor Kay's laboratory has also developed the theoretical framework for the important step of relating protein dynamics to thermodynamics. The methods developed in his laboratory have been used by his group and others to study molecular recognition, protein stability and the energetics of ligand binding. His group has also developed methods for studying the invisible excited states of proteins by NMR and is applying them to furthering our understanding of protein folding and conformational dynamics. Lewis Kay's contributions will continue to provide insights into protein structures and their fluctuations that will carry on elucidating further their biological functions for many years to come.
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