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Phillip Stansfeld

Associate Professor


Phillip Stansfeld

Phillip is Associate Professor in both the School of Life Sciences and the Department of Chemistry

Phillip dot Stansfeld at warwick dot ac dot uk

024 765 23864

Office B008

Dr Phillip Stansfeld Research Group

Groups at Warwick


Affiliations

  • School of Life Sciences

Biography

  • 2003 Bsc with Hons (1st Class) Biological Sciences, University of Edinburgh
  • 2007 PhD Biochemistry, University of Leicester
  • 2007-2010 Wellcome Trust Postdoc, University of Oxford
  • 2011-2014 BBSRC Researcher Co-Investigator, University of Oxford
  • 2015-2019 Research Fellow, University of Oxford
  • 2019- Associate Professor (Reader) Computational Biochemistry, University of Warwick

I am working on the following projects at the moment:

  • Lipoprotein Biogenesis Pathway
  • LipID: Lipid Interactions with Membrane Proteins
  • Twin Arginine Translocase
  • KATP Potassium Channel
  • Bacterial Chemotaxis
  • Surface-Layer Proteins

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, drug molecules and other components of the protein complexes.

Phillip teaches the CH3F1 undergraduate module


I am supervising the following PhD students:

  • Martin McAndrew (MRC DTP)
  • Chelsea Brown (MRC DTP)
  • Joshua Sauer (Oxford)
  • Will Pipatpolkai (Oxford)
  • Dan Quetschlich (Oxford/UCB)
  • Patrick Simcock (Oxford/IBM)
  • Michael Horrell (Oxford/UCB)

Please get in touch if you would like to join the team.

Journals

Further Publications