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George Hedger |
Structural Bioinformatics and Computational Biochemistry Unit Dept. of Biochemistry University of Oxford South Parks Road Oxford OX1 3QU U.K. Telephone: 01865 613304 Fax: 01865 613238 e-mail: george.hedger@lincoln.ox.ac.uk |
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Characterising lipid-protein interactions through computational modelling | |
Background |
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I obtained my undergraduate degree in Biochemistry from the University of Oxford in 2014. My final year masters project involved investigating lipid interactions of the human receptor tyrosine kinase (hRTK) family of membrane proteins, and was supervised by Dr Heidi Koldsø.
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Research |
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My research involves application of molecular dynamics to probe the lipid interactions of biomedically important membrane proteins. The current focus of my research is on the interactions of the epidermal growth factor receptor (EGFR) and the Insulin receptor (IR) with the modulatory glycolipid GM3 and the phosphoinositide PIP2 at the plasma membrane. Additionally, I am working on projects examining cardiolipin interactions with the ADP/ATP carrier (AAC1/ANT) within the inner membrane of mitochondria. | |
Publications |
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Hedger, G.; Shorthouse, D.; Koldsø, H.; Sansom, M. S. P. (2016) Free energy landscape of lipid interactions with regulatory binding sites on the transmembrane domain of the EGF receptor.
Hedger, G.; Sansom, M. S. P. (2016) Lipid interaction sites on channels, transporters and receptors: Recent insights from molecular dynamics simulations.
Byrne, E. F. X.; Sircar, R.; Miller, P. S.; Hedger, G.; Luchetti, G.; Nachtergaele, S.; Tully, M. D.; Mydock-McGrane, L.; Covey, D. F.; Rambo, R. P.; Sansom, M. S. P.; Newstead, S.; Rohatgi, R.; Siebold, C. (2016) Structural basis of smoothened regulation by its extracellular domains.
Shorthouse, D.; Hedger, G.; Koldsø, H.; Sansom, M. S. P. (2016) Molecular simulations of glycolipids: Towards mammalian cell membrane models.
Hedger, G.; Sansom, M. S. P.; Koldsø, H. (2015) The juxtamembrane regions of human receptor tyrosine kinases exhibit conserved interaction sites with anionic lipids. |
Last updated &&/&&/07 |