Metal-switched bifunctionality explains the mysterious half-sites reactivity of glyoxalase I enzymes — ASN Events

Metal-switched bifunctionality explains the mysterious half-sites reactivity of glyoxalase I enzymes — ASN Events

Metal-switched bifunctionality explains the mysterious half-sites reactivity of glyoxalase I enzymes

Metal-switched bifunctionality explains the mysterious half-sites reactivity of glyoxalase I enzymes (#205)

Rohan Bythell-Douglas ¹ , Uthiawan Suttisansanee ² , John Honek ³ , Charles S Bond ¹

University of Western Australia, Crawley, WA, Australia
Mahidol University, Nakhon Pathom, Thailand
Dept of Chemistry, University of Waterloo, Waterloo, Ontario, Canada

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Authors contributing to this presentation.

Bythell-Douglas, R

Suttisansanee, U

Honek, J

Bond, C.S

I want to understand how the spatial arrangement of biological molecules in complexes dictates their function. I am particularly interested in protein:nucleic acid interactions, and their functions in gene regulatory complexes in eukaryotes. I love collaborating, to combine my expertise in crystallography, bioinformatics, biochemistry and molecular biology, with experts in cell biology and other biophysical techniques.