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A combined magnetic resonance (NMR and EPR) approach to identifying and characterising ligand interactions. (MACMILLANF1U20SF)

Project Description

We use advanced magnetic resonance approaches to identify and characterise weak molecular interactions. The aim of this project is to combine both Electron Paramagnetic Resonance (EPR) and Nuclear Magnetic Resonance (NMR) spectroscopic techniques to study such interactions. Modern EPR spectroscopy is quickly moving from being a rather niche technique to a key structurual tool by providing accurate distance information in the nanometer range. Since this is outside the range of typical NOE-based NMR experiments, there is an opportunity to utilise these two techniques in combination to provide unique structural information, especially about dynamic macromolecules.

This PhD project will use specific biomacromolecular machines which are structurally dynamic and where key functional information relies on understanding the distribution of their various conformational states. We aim to develop and this novel methodology and to then apply it to probe the functional dynamics of these machines using a combination of state-of-the-art magnetic resonance (specifically STD-NMR and PELDOR) techniques in different solvent matrices using a range of both endogenous and exogenous spin probes.

The successful candidate will join the Henry Wellcome Unit for Biological EPR research team, which together with the UEA NMR facility makes up the core of magnetic resonance infrastructure on the Norwich Research Park. You will be trained to become expert in magnetic resonance spectroscopy with skills in data simulation, spin probe chemistry, isotope labelling and biological chemistry.

For more information about the supervisor of this programme please visit

This is a PhD programme, the start date is October 2020.

The study mode is full time

Acceptable first degree in chemistry, physics, biophysics or related. The standard minimum entry requirement is 2:1

Funding Notes

This PhD project is offered on a self-funding basis. It is open to applicants with funding or those applying to funding sources. Details of tuition fees can be found at View Website.

A bench fee is also payable on top of the tuition fee to cover specialist equipment or laboratory costs required for the research. Applicants should contact the primary supervisor for further information about the fee associated with the project.


i) Mullen, A.; Hall, J.; Diegel, J.; Hassan, I.; Fey, A.; MacMillan, F. Membrane transporters studied by EPR spectroscopy: structure determination and elucidation of functional dynamics. Biochem. Soc. Trans. 2016, 44, 905–915.
ii) Claxton, D. P.; Kazmier, K.; Mishra, S.; Mchaourab, H. S. Navigating Membrane Protein Structure, Dynamics, and Energy Landscapes Using Spin Labelling and EPR Spectroscopy. Meth. Enzymol. 2015, 564, 349–387
iii) M. Mayer, B. Meyer, Characterization of Ligand Binding by Saturation Transfer Difference NMR Spectroscopy, Angew. Chem. Int. Ed. 1999, 38, 1784-1788.
iv) Claridge, T.D.W, Protein Ligand Screening by NMR in High-Resolution NMR techniques, Chapter 11, Elsevier, Amsterdam (2016)

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