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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Sylvia McLain
Structural investigations in solution on drugs, lipids and peptides on the atomic scale

Co-workers:  Dr. Richard Gillams, Dr. Natasha Rhys, Ms. Nicola Steinke, Mr. Thomas Dixon, Ms. Rachel McCann, Ms. Imogen Duffy

Group research website: McLain Group website


We are interested in understanding the interactions between biological molecules at the atomic level in physiologically relevant environments. We use a combination of neutron scattering, NMR and computer simulation to probe the interplay between these molecules on the atomic and molecular level (Å (10-10 metres)) to the nanoscale (10-9metres).  

Currently we are focusing on understanding the interactions between biological molecules - such as peptides and lipids - and the surrounding aqueous environment.  We use two experimental techniques - local structural neutron diffraction (LSND) and high resolution NMR. 

These experimental measurements are complemented with computer modelling techniques (MD and Empirical Potential Structure Refinement (EPSR)) to investigate how the atomic scale structure and dynamics link to larger structures on the nanometre length scale.

 

For more information about our research, current group members and research publications please visit the  McLain Group website


 

 

 

 

Recent Publications

  1. Henao, A., Johnston, A. J., Guardia, E., McLain, S. E. and Pardo, L. C. (2016) On the positional and orientational order of water and methanol around indole: a microscopic orgin of solubility Phys. Chem. Chem. Phys., 18, 23006-23016 doi:10.1039/C6CP04183C
  2. Sridhar, A., Johnston, A. J.,Varathan, L., McLain, S.E and Biggin, P.C. (2016) The solvation structure of alprazolam Phys. Chem. Chem. Phys., 18, 22416-22425 doi:10.1039/C6P02645A
  3. Gillams, R. J., Lorenz, C. D. and McLain, S. E. (2016) Comparative atomic-scale hydration of the ceramide and phosphocholine headgroup in solution and bilayer environments J. Chem. Phys. 144, 225101 doi:10.1063/1.4952444
  4. Steinke, N., Gillams, R. J., Pardo, L. C., Lorenz, C. D. and McLain, S. E. (2016) Atomic scale insights into urea-peptide interactions in solution  Phys. Chem. Chem. Phys., 18, 3862-3870. DOI: 10.1039/C5CP06646H
  5. Johnston, A. J., Busch, S., Pardo, L. C., Callear, S. K., Biggin, P. C. and McLain, S. E. (2016) On the Atomic Structure of Cocaine in Solution Phys. Chem. Chem. Phys., 19 991 - 999.doi:10.1039/C5CP06090G
  6. Johston, A. J., Zhang, Y. R, Busch, S., Pardo, L. C. and McLain, S. E. (2015) Amphipathic Solvation of Indole: Implications for the Role of Tryptophan in Membrane Proteins J. Phys. Chem. B, 119 (19), 5979-5987. doi:10.1021/acs.jpcb.5b02476
  7. Gillams, R. J., Busto, J. V., Busch, S., Goñi, F. M., Lorenz, C. D. and McLain, S. E. (2015) Solvation and hydration of the ceramide headgroup in a non-polar solution. J. Phys. Chem. B, 119 (1) 128-135. doi:10.1021/jp5107789
  8. Busch, S., Lorenz, C.D., Taylor, J.W., Pardo, L.C. and McLain, S.E. (2014) Short range interactions of concentrated proline in aqueous solution.  J. Phys. Chem. B., 118 (49), 14267-14277. doi: 10.1021/jp508779d
  9. Busch, S., Bruce, C.D.,Redfield, C., Lorenz, C.D. and McLain, S.E. (2013)  Water mediation essential to nucleation of ß-turn formation in peptide folding motifs. Angew. Chem. Int. Ed., 52 (49), 13091 - 13095.  doi:10/1002/ange.201307657
  10. Busch, S., Pardo, L.C., Redfield, C., Lorenz, C.D. and McLain, S.E. (2013) On the structure of water and chloride ion interactions with a peptide backbone in solution. Phys. Chem. Chem. Phys., 15, 21023-21033. doi:10.1039/C3CP5831A
Full publication list...

Research Images

The probability distribution of water (left) around cocaine showing the top 30% of water molecules with in a distance range of 0-4 Å from any atom in the cocaine molecules. The molecules in the center of the plot show the range of different conformations of cocaine through-out the EPSR simulations of the neutron data. The most likely orientation of water molecules (right panel) within the distribution shell shown in the left panel.  This orientation suggests that the amine and carbomethyoxy groups in cocaine are held together or strongly associate with water molecules.  This hydration and conformation of cocaine suggests a mechanism of interaction between cocaine and the BBB that negates the need for deprotonation prior to interaction with the lipophilic portions of this barrier, that is water helps the cocaine molecule to 'fold up' protecting its charged portions in a lipophlilic environment. (AJ Johnston, et al. PCCP (2016))

 


 

Water-mediated ceramide head group interactions for ceramide and water in a non-polar solution showing a water molecule simultaneously bound to both the carbonly of the amide group and a hydroxyl group. (RJ Gillams et al. J. Phys. Chem, B (2015))

Water-mediation observed to be essential to the nucleation of ß-turn formation for peptides in solution.  The figure shows representative water-mediated turns for the peptide glycine-proline-glycinamide (GPG) in aqueous solution.  The red dotted line represents water mediated turns observed from computer simulations of neutron diffraction data and the blue line represents water-mediated turns from MD simulations.   (S. Busch, et al. Agnew. Chem. Int. Ed. (2013))


 

Contact:sylvia.mclain@bioch.ox.ac.uk

Positions available:

Group website: McLain group website