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个人简介
Research in my laboratory focuses on understanding what determines how proteins change conformation, which for example underpins such diverse events as enzyme catalysis and amyloid formation. We use a wide range of structural biology and molecular biophysics approaches, from multi-dimensional NMR, EM and X-ray crystallography to laser photolysis and rapid kinetics, to build a comprehensive picture of how proteins behave under different conditions, and how this behavior can be perturbed by therapeutics. Current projects include unraveling the multitude of steps that occur during enzyme catalysis of phosphate group transfer. Phosphate transfer is essential in almost all processes of life, which make these enzymes highly prized therapeutic targets. In parallel, we are examining the equivalent catalysis of methyl group transfer, which presents an enzyme with very different challenges. These enzymes are also high value therapeutic targets. In the protein folding-misfolding area we are currently developing methods that enable the detailed characterization of intrinsically disordered proteins, and examining how a promising biotherapeutic for the treatment of a wide range of neurodegenerative disorders is causing amyloid removal. All of these projects are supported through funding from UK research councils and the Pharma sector.
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Fabio Falcioni, Robert W Molt, Yi Jin,Jonathan P Waltho, Sam Hay,Nigel G J Richards, G Michael Blackburn
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D-Core
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