Professor of Nuclear Magnetic Resonance Spectroscopy.
Tim is Director of the NMR facilities for Organic Chemistry and Chemical Biology.
Book: High-Resolution NMR Techniques in Organic Chemistry
High-Resolution NMR Techniques in Organic Chemistry, Third Edition describes the most important NMR spectroscopy techniques for the structure elucidation of organic molecules and the investigation of their behaviour in solution. Appropriate for advanced undergraduate and graduate students, research chemists and NMR facility managers, this thorough revision covers practical aspects of NMR techniques and instrumentation, data collection, and spectrum interpretation. It describes all major classes of one- and two-dimensional NMR experiments including homonuclear and heteronuclear correlations, the nuclear Overhauser effect, diffusion measurements, and techniques for studying protein–ligand interactions. A trusted authority on this critical expertise, High-Resolution NMR Techniques in Organic Chemistry, Third Edition is an essential resource for every chemist and NMR spectroscopist.
My research interests revolve around the application of solution-state NMR techniques to address questions of structure, function and dynamics of "small" molecules in organic chemistry and chemical biology. Many of the projects in which I become involved arise through collaborations with groups across the department and the university more widely.
NMR Supersequences for efficient structure characterisation: NOAH
I am involved with the development of time-efficient NMR "supersequences" termed NOAH (NMR by Ordered Acquisition using 1H detection) that can provide a significant reduction in the time required for collecting 2D data sets used for the characterisation of small molecules. These experiments work by nesting multiple conventional 2D experiments into one, thereby reducing the number of lengthy magnetisation recovery delays required in data acquisition. This work is in collaboration with Eriks Kupce of Bruker Biospin UK. See our NOAH page for more details and access to pulse programs etc.
Protein-ligand binding studies by NMR Spectroscopy
The interaction of small molecules with protein targets is an area in which NMR spectroscopy can play a key role, providing information on the behaviour of the small molecule and on structural changes in the protein itself. A wide range of techniques are available to probe such interactions (such as relaxation filtering, saturation transfer difference and WaterLOGSY) and we are interested in further developing and applying such methods to a variety biological systems. We also employ protein-observe methods when isotopically labelled macromolecules are available, for example via non-specific15N or specific19F labelling.
NMR methods for studying small molecules
Despite their relatively small size, many molecules encountered in the laboratory of synthetic and medicinal chemists have structures that can prove surprisingly difficult to define reliably, especially in relation to stereochemistry. We are interested in exploring the application of novel methods and developing these further to help better elucidate small molecule structures. Methods that are currently of interest are those based on pure shift methodology (broadband proton decoupled proton spectroscopy), methods for fluorinated molecules, the use of anisotropic parameters as alternatives to traditional scalar couplings and NOEs.
Details of my book and journal publications are provided here.
My first degree was in "Chemistry and Analytical Science" at Loughborough University, which included a "sandwich" year in the spectroscopy laboratory at (what was then) Beecham Pharmaceuticals (now part of GlaxoSmithKline). During this time I gained experience of hands-on NMR and discovered this to be infinitely more interesting than chromatography so decided that a Ph.D in NMR was my next goal. This was completed in Oxford under the supervision of the late Andy Derome, during which I was a member of Wolfson College (an Oxford graduate college).
In 1992 I was appointed as the NMR Facility Manager in the Dyson Perrins Laboratory.
In 2004 the Facility moved in to the Chemistry Research Laboratory and I became the Facility Director for Organic Chemistry and Chemical Biology.
In 2006 I was als awarded the title of University Research Lecturer and in 2014 became Professor of Nuclear Magnetic Resonance.
For the period 1998- 2009 I served on the committee of the UK Royal Society of Chemistry NMR Discussion Group and was its Chairman from 2006-2009. In 2012 I co-founded the UK Magnetic Resonance Managers (UKMRM) group (with Dr Craig Butts, University of Bristol) and currently serve on the organising committee of the SMASH (Small Molecules Are Still Hot) International NMR conference and on the Advisory Board for the journal Magnetic Resonance in Chemistry.