My research spans the disciplines of Chemistry and Biology, with a focus on the structural enzymology and chemical biology of proteins involved in the synthesis and degradation of carbohydrates. Current projects include:
Selected Recent Publications
- Spectroscopic and computational insight into the activation of O2 by the mononuclear Cu center in polysaccharide monooxygenases
C Kjaergaard et al., Proc Natl Acad Sci (USA) 2014. 111, 8797-8802.
- A discrete genetic locus confers xyloglucan metabolism in select human gut Bacteroidetes
J Larsbrink et al., Nature 2014 506, 498-502
- Discovery and characterization of a new family of lytic polysaccharide monooxygenases
G R Hemsworth et al., Nature Chem Biol. 2014. 10, 122-126
- Combined inhibitor free energy landscape and structural analysis reports on the mannosidase conformational coordinate
R J Williams et al., Angew Chemie Int Ed. 2014, 53, 1087-1091.
- The Copper Active Site of CBM33 Polysaccharide Oxygenases.
G R Hemsworth et al. J Am Chem Soc. 2013, 135, 6069-6077.
- Structural and mechanistic insight into N-glycan processing by endo-α-mannosidase.
A J Thompson et al., Proc Natl Acad Sci (USA), 2012, 109, 781-786.
- Visualizing the reaction coordinate of an O-GlcNAc hydrolase.
Y He et al., J Am Chem Soc, 2010, 132, 1807-1809.
Gideon Davies received his PhD from the University of Bristol in 1990 with postdoctoral research at EMBL Hamburg and CNRS Grenoble. In 1996 he received a Royal Society University Research Fellowship to work on Carbohydrate-Active Enzymes. He was made a Professor of the University of York in 2001. Professor Davies has won many awards including the 2014 Khorana Prize of the Royal Society of Chemistry, the 2010 Gabor Medal of the Royal Society and the 2010 GlaxoSmithKline award of the Biochemical Society and the Whistler Prize of International Carbohydrate Organisation. Gideon was elected a member of the European Molecular Biology Organization, a Fellow of The Royal Society in 2010 and a Fellow of the Academy of Medical Sciences in 2014.
Proc Natl Acad Sci (USA) 111, 8797-8802.