Department of Biochemistry University of Oxford Department of Biochemistry
University of Oxford
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Oxford OX1 3QU

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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
Image showing the global movement of lipids in a model planar membrane
Matthieu Chavent, Sansom lab
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Award for new group leader Dr Sylvia McLain

One of the department’s most recently established group leaders, Dr Sylvia McLain, has won the prestigious B.T.M Willis prize awarded annually by the Neutron Scattering Group of the Institute of Physics and the Royal Society of Chemistry.

Neutron scattering is normally considered a physics technique, but Dr McLain uses it to understand fundamental biological problems. The B.T.M Willis prize recognises her studies of a wide range of biological molecules and their interactions at the atomic and molecular level in the presence of water.

Dr Sylvia McLain receiving the prize

Dr Sylvia McLain receiving the prize (Click to enlarge)

Dr Ali Zarbakhsh, Chair of the Neutron Scattering Group, said: ‘We were impressed with Sylvia’s research which is of wide interest and importance to academic research and several medical industries including pharmaceuticals. She has expanded the level of structural details we can obtain using neutron scattering techniques and advanced the complexity of the systems we can study.’

Dr McLain joined the department from King’s College London last October having been awarded an EPSRC Career Acceleration Fellowship. She was one of 30 outstanding researchers to receive these awards in 2011 which will help them develop their potential as the next generation of world-leading scientists and engineers.

The Fellowship provides five years generous funding for Dr McLain to build up a lab and establish an independent career. She will be pursuing research on ‘the physics of life’ – looking at the atomic structural scale in solution, a physiologically relevant environment.

‘I’m applying this to membrane formation and protein folding in particular,’ says Dr McLain, ‘looking at the physics behind how this happens and trying to place that in the wider biological context. Ultimately, we would like to see how complex molecules cross a cellular membrane - how peptides and bioactive proteins actually associate with the membrane.’

‘We start with fairly simple models such as lipids in a hydrophobic environment, systems that we can characterise quite well. Then we slowly add very small amounts of water to these systems to understand how hydration changes the atomic structure and dynamics of these simple systems.’

‘The bigger picture is how molecules associate in biology. Association in solutions underlies everything in biology – membrane formation, protein folding, how drugs bind to ligand receptors. Nobody fully understands the physics of how these happen in water.’

The behaviour of molecules in water is difficult to probe using most standard techniques – NMR, for example, is not sensitive to hydrogen bonds which are formed with water. Researchers mostly look at structure using crystallography, but an X-ray crystallographic structure of a protein does not necessarily translate into its structure in solution.

Peptide clusters in solution (from Molecular Dynamics simulations)

Peptide clusters in solution (from Molecular Dynamics simulations) (Click to enlarge)

Dr McLain’s approach combines neutron scattering with other techniques. ‘We are trying to take a technique that has traditionally been used to study very simple molecules and use that in concert with standard biophysical techniques to look at water hydration around molecules and the structure of molecules in solution. We can measure things like hydrogen bonds really well with neutrons. So we want to combine all of these techniques to give a greater understanding of structures in solution.’

She will use a range of techniques – neutrons on solution, X-ray on solutions, solid-state NMR and NMR in solution, as well as computer simulation – to try and understand the details of water interactions.

The limited amount of work that has been done in the area indicates how important the problem is. ‘People just thought that water was excluded when drugs bind into pockets in a protein,’ says Dr McLain, ‘but they are finding that there is water actually in the crystal structures in important binding sites.’


Pharmaceutical companies know little about how their drugs work at the molecular level. This type of work would provide valuable information and could be used, for example, to help design drugs that can be targeted for delivery to specific cell types.

Dr McLain says that Oxford and the department offer a stimulating environment for her research. She already collaborates with many departmental researchers including Professors Anthony Watts, Mark Sansom, and Christina Redfield, and Dr Phil Biggin, and will benefit from access to good facilities and the presence of excellent students.

A better understanding of the underlying interactions of molecules in solution will eventually help to build up a picture of the bigger, cellular structures in biology - connecting what is happening on a molecular level all the way up to a physiological level.

Trying to connect this together is the real challenge, says Dr McLain. ‘That is why this Department is a good place for me to be.’



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