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User:Darrell Cockburn
Darrell Cockburn received his BSc. and PhD from the University of Guelph in Ontario, Canada. During his PhD under his adviser ^^^Anthony Clarke^^^, Darrell primarily studied the structure function relationships within the endoglucanase family GH6. In 2010 Darrell moved to Denmark to take an H.C. Ørsted fellowship with ^^^Birte Svensson^^^ at the Technical University of Denmark. There he studied surface binding sites in a variety of carbohydrate active enzymes, with a particular focus on GH13. In 2013 Darrell moved to the University of Michigan to continue his Postdoctoral training with Nicole Koropatkin, studying the amylolytic systems of the gut bacteria Eubacterium rectale and Ruminococcus bromii.
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Cockburn, D., Wilkens, C., Ruzanski, C., Andersen, S., Willum Nielsen, J., Smith, A.M., Field, R.A., Willemoës, M., Abou Hachem, M., and Svensson B. (2014) Analysis of surface binding sites (SBSs) in carbohydrate active enzymes with focus on glycoside hydrolase families 13 and 77 — a mini-review. Biologia, 69, 705-712. DOI: 10.2478/s11756-014-0373-9
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Cockburn, D. and Svensson, B. Surface binding sites in carbohydrate active enzymes: an emerging picture of structural and functional diversity. 2013. In: Lindhorst TK, Rauter AP (eds) SPR carbohydrate chemistry—chemical and biological approaches, vol 39. Royal Society of Chemistry, Cambridge. DOI: 10.1039/9781849737173-00204
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Møller, M.S., Cockburn, D., Nielsen, J.W., Jensen, J.M., Vester-Christensen, M.B., Nielsen, M.M., Andersen, J.M., Wilkens, C., Rannes, J., Hägglund, P., Henriksen, A., Abou Hachem, M., Willemoës M., and B. Svensson (2013) Surface Binding Sites (SBS), Mechanism and Regulation of 2 Enzymes Degrading Amylopectin and α-limit Dextrins. J. Appl. Glycosci. EPub March 21. DOI: 10.5458/jag.jag.JAG-2012_023
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Diemer, S.K., Svensson, B., Nygren Babol, L., Cockburn, D., Grijpstra, P., Dijkhuizen, L., Folkenberg, D.M., Garrigues, C., and R. Ipsen (2012) Binding interactions between α-glucans from Lactobacillus reuteri and milk proteins characterised by surface plasmon resonance. Food Biophys. 7: 220-226. DOI: 10.1007/s11483-012-9260-5
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