CAZypedia needs your help! We have many unassigned GH, PL, CE, AA, GT, and CBM pages in need of Authors and Responsible Curators.
Scientists at all career stages, including students, are welcome to contribute to CAZypedia. Read more here, and in the 10th anniversary article in Glycobiology.
New to the CAZy classification? Read this first.
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Consider attending the 15th Carbohydrate Bioengineering Meeting in Ghent, 5-8 May 2024.
Difference between revisions of "User:Harry Gilbert"
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| − | After working at Newcastle University since 1985 I | + | After working at Newcastle University since 1985 I moved (November 2008) to the Complex Carbohydrate Research Center at the University of Georgia in Athens, USA, returning to Newcastle University in November 2010. My major research interests are focused on enzymes that modify complex carbohydrates. I am interested in glycoside hydrolases and glycosyltransferases. I also have a generic interest in the mechanism of carbohydrate-protein recognition using non-catalytic carbohydrate binding modules (CBMs) as my model system. My research is focused on understanding the catalytic mechanism and the structural basis for the substrate specificity displayed by these enzymes. We use a combination of structural biology, primarily X-ray crystallography but also NMR, to determine the three dimensional structure of these enzymes, in combination with rational design and forced protein evolution to dissect how these enzymes work. |
Latest revision as of 09:18, 30 April 2012
After working at Newcastle University since 1985 I moved (November 2008) to the Complex Carbohydrate Research Center at the University of Georgia in Athens, USA, returning to Newcastle University in November 2010. My major research interests are focused on enzymes that modify complex carbohydrates. I am interested in glycoside hydrolases and glycosyltransferases. I also have a generic interest in the mechanism of carbohydrate-protein recognition using non-catalytic carbohydrate binding modules (CBMs) as my model system. My research is focused on understanding the catalytic mechanism and the structural basis for the substrate specificity displayed by these enzymes. We use a combination of structural biology, primarily X-ray crystallography but also NMR, to determine the three dimensional structure of these enzymes, in combination with rational design and forced protein evolution to dissect how these enzymes work.