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
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Theses and Reports


Year Author Title
2014 Steven Lavington
2015 Alice Hart
The Role of β-Arrestin Finger Loop
Residues in GPCR Binding Affinity
2015 Patricia Dijkman

Biophysical Studies of Membrane Protein Structure and Function

2014 Roslin Adamson Probing GPCR-Gα interactions : a functional study by EM and SPR
2012 Olivia Berthoumieu

Single Molecule Studies of Seven Transmembrane Domain Proteins

2011 Marcella Orwick Biophysical and Magnetic Resonance Studies of Membrane Proteins
2009 Satita Tapaneeyakorn Towards NMR spectrocopic studies of the NTS1-NT complex
2008 Peter Judge Kinetics and modulation of the viral ion channel VPU from HIV-1
2007 Lubica Aslimovska High resolution structural studies of membrane proteins using solid state NMR
2007 Peter Harding A biophysical study of the G-protein coupled receptor neurotensin receptor 1
2006 Timothy Hadingham Biophysical studies of the G-protein coupled neurotensin receptor
2005 Chang Gyeom Kim Probing structures of membrane proteins and their inhibitors
2004 Vincent Lemaitre Non-covalent interactions in biomolecules studied by 17O NMR and MD simulations
2003 Jonathan Sharples The conformation of the β-ionone ring region of the chromophore of rhodopsin, in the dark and meta-I photostates
2002 Scott Goodall Probing the structure of acetylcholinesterase inhibitors in their binding site using solid state nuclear magnetic resonance
2001 James Mason Solid-state NMR Studies of bacteriorhodopsin and the purple membrane
2001 Jude Watts Probing inhibitor binding sites of the gastric H/K-ATPase
2000 Zareen Ahmed Magnetic resonance spectroscopy of phospholamban and its interaction with Ca2+-ATPase
1999 Phil Williamson The application of solid state nuclear magnetic resonance to the study of ligand protein interactions
1998 Clemens Glaubitz Probing structures of membrane proteins and their inhibitors
















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