Department of Biochemistry University of Oxford Department of Biochemistry
University of Oxford
South Parks Road
Oxford OX1 3QU

Tel: +44 (0)1865 613200
Fax: +44 (0)1865 613201
Image showing the global movement of lipids in a model planar membrane
Matthieu Chavent, Sansom lab
Anaphase bridges in fission yeast cells
Whitby lab
Lactose permease represented using bending cylinders in Bendix software
Caroline Dahl, Sansom lab
Epithelial cells in C. elegans showing a seam cell that failed to undergo cytokinesis
Serena Ding, Woollard lab
Collage of Drosophila third instar larva optic lobe
Lu Yang, Davis lab
First year Biochemistry students at a practical class
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Phillip Stansfeld
Computational Biochemistry of Membrane Proteins

Co-workers: Thomas Newport, Nick Michelarakis, Jan Domanski, Sophie Williams, Jodie Ford, Daniel Quetschlich, Matt Raybould, Ben Mynors-Wallis, Tom Dyer


One of the fundamental challenges in biological sciences is to visualise biomolecular machines in high-resolution detail. This is notoriously difficult, expensive and time-consuming to achieve by using experimental techniques, especially for proteins that exist in cell membranes, known as Integral membrane proteins (IMPs). These proteins play fundamental roles in cell biology e.g. as processing enzymes, ion channels, drug receptors, and solute transporters.

My group uses computational methods to study IMP structures and currently hosts MemProtMD; a pipeline for inserting experimentally-solved IMP structures into their native bilayer environment and analysing the stability, dynamics and resultant lipid interactions. This resource uses multiscale molecular dynamics (MD) simulations that permit the accurate assembly of an IMP into a membrane at the coarse-grain level, prior to careful assessment of the quality of the IMP structure at atomic resolution.

The MemProtMD pipeline also forms a springboard to studying the dynamics of experimentally solved structures through MD simulations.

With the increasing threat of anti-microbial resistance, we are especially interested in bacterial IMPs. Knowledge of the three-dimensional structures of proteins involved in essential processes provides the physical details of potentially viable targets for killing drug-resistant, pathogenic bacteria. By breathing life into these frozen structures we may assess the association of proteins with lipids, substrates, drug molecules and other components of the protein complexes.


Computational/bioinformatics studies:

  1. Alcock F*, Stansfeld PJ*, Basit H, Habersetzer J, Baker MA, Palmer T, Wallace MI, Berks BC. Assembling the Tat protein translocase. Elife. 2016 5: e20718.
  2. Stansfeld P.J., Goose, J.E., Caffrey, M., Carpenter, E.P., Parker, J.L., Newstead, S., Sansom M.S.P. (2015) Mem ProtMD: Automated Insertion of Membrane Protein Structures into Explicit Lipid Membranes. Structure. 23:1350-1361.
  3. Stansfeld P.J., Jefferys E.E., Sansom M.S.P. (2013) Multiscale simulations reveal conserved patterns of lipid interactions with aquaporins. Structure. 21:810-819.
  4. Stansfeld P.J., Sansom M.S.P. (2011) From coarse grained to atomistic: a serial multiscale approach to membrane protein simulations. J. Chem. Theory Comput. 7: 1157-1166
  5. Stansfeld, P.J., Hopkinson, R., Ashcroft, F.M. & Sansom, M.S.P. (2009) The PIP2 binding site in Kir channels: definition by multiscale biomolecular simulations. Biochem. 48:10926-10933

Recent Collaborations:

  1. Wiktor M, Weichert D, Howe N, Huang CY, Olieric V, Boland C, Bailey J, Vogeley L, Stansfeld PJ, Buddelmeijer N, Wang M, Caffrey M. Structural insights into the mechanism of the membrane integral N-acyltransferase step in bacterial lipoprotein synthesis. Nat Commun. 2017. 8:15952.
  2. Gupta K, Donlan JAC, Hopper JTS, Uzdavinys P, Landreh M, Struwe WB, Drew D, Baldwin AJ, Stansfeld PJ, Robinson CV. The role of interfacial lipids in stabilizing membrane protein oligomers. Nature. 2017 541:421.
  3. Gu Y, Li H, Dong H, Zeng Y, Zhang Z, Paterson NG, Stansfeld P.J., Wang Z, Zhang Y, Wang W, Dong C. Structural basis of outer membrane protein insertion by the BAM complex. Nature, 2016. 531:64.
  4. Vogeley, L, El Arnaout, T, Bailey, J, Stansfeld P.J., Boland, C, Caffrey, M. Structural basis of lipoprotein signal peptidase II action and inhibition by the antibiotic globomycin. Science, 2016. 351:876.
  5. Li, D, Stansfeld P.J., Sansom, M.S., Caffrey, M. (2015) Ternary structure reveals mechanism of a membrane diacylglycerol kinase. Nature Communications. 6:10140.
  6. Dong, H., Xiang, Q., Gu, Y., Wang, Z., Paterson, N.G., Stansfeld, P.J., He, C., Zhang, Y., Wang, W., & Dong, C. (2014) Structural basis for outer membrane lipopolysaccharide insertion. Nature 511: 52-56.
  7. Rollauer, SE, Tarry, MJ, Graham, JE, Jaaskelainen, M, Jager, F, Johnson, S, Krehenbrink, M, Liu, SM, Lukey, MJ, Marcoux, J, McDowell, MA, Rodriguez, F, Roversi, P, Stansfeld, P.J., Robinson, CV, Sansom, MS, Palmer, T, Hogbom, M, Berks, BC, Lea, SM, Structure of the TatC core of the twin-arginine protein transport system. Nature, 2012. 492: 210.
  8. Quigley, A, Dong, YY, Pike, AC, Dong, L, Shres tha, L, Berridge, G, Stansfeld, P.J., Sansom, MS, Edwards, AM, Bountra, C, von Delft, F, Bullock, AN, Burgess-Brown, NA, Carpenter, EP, The structural basis of ZMPSTE24-dependent laminopathies. Science, 2013. 339:1604.

Review Articles:

  1. Stansfeld PJ. Computational studies of membrane proteins: from sequence to structure to simulation. Curr Opin Struct Biol. 2017. 45:133.
  2. Berks BC, Lea SM, Stansfeld PJ. Structural biology of Tat protein transport. Curr Opin Struct Biol. 2014. 27:32.
  3. Stansfeld PJ, Sansom MS. Molecular simulation approaches to membrane proteins. Structure. 2011 19:1562.


Graduate Student and Postdoctoral Positions: Enquiries with CV welcome