Email: mark.sansom@bioch.ox.ac.uk
Personal Biography
I was born in Stourbridge and grew up in the West Midlands, and later on in West Yorkshire, where I attended a local grammar school in Normanton before going to University College, Oxford to study Biochemistry. So, right from the outset I benefitted from the tutorial system and from the Oxford Biochemistry course. I did my D.Phil. in protein structure with Prof. Louise Johnson (the previous David Phillips Professor of Molecular Biophysics at Corpus) before going to Nottingham University as a postdoctoral research fellow to work on ion channels. I stayed at Nottingham as a lecturer and then a research fellow for 7 years before returning to Oxford. I was a university lecturer in Biochemistry and a college tutor at Christ Church for 20 years. In 2011 I was made the David Phillips Professor of Molecular Biophysics, and moved to Corpus as a Professorial fellow. From 2011 to 2018 I was also the Head of the Biochemistry Department.
Research
I head a research group of ~20 people using computational approaches to understand the relationship between the structure and function of membrane proteins. We are particularly interested in two areas: the interaction of membrane proteins with lipids [1]; and the role of water molecules in the function of ion channels [2]. My research is currently funded by Wellcome, BBSRC and EPSRC, and is relevant to the pharmaceutical and computational industries.
I lecture within the Biochemistry department on the relationship between structure and function in membrane proteins, and also on the use of computational methods to study proteins.
Selected Publications
[1] Duncan, A., Song, W. & Sansom, M.S.P. (2020) Lipid-dependent regulation of ion channels and GPCRs: insights from structures and simulations. Ann. Rev. Pharmacol. Toxicol. 60:20.1
[2] Rao, S., Klesse, G., Stansfeld, P.J., Tucker, S.J., & Sansom, M.S.P. (2019) A heuristic derived from analysis of the ion channel structural proteome permits the rapid identification of hydrophobic gates. Proc. Natl. Acad. Sci. USA 116: 13989