Profile
Biography
Neil graduated in Natural Sciences from Fitzwilliam College, University of Cambridge in 1997 and remained in Cambridge to complete his PhD in Diode Laser Spectroscopy of Transient Species with Professor Paul Davies in 2000. Following his PhD Neil moved to a Welsh postdoctoral Fellowship at Rice University, Houston working with Professor R F Curl. Following further post-doctoral study in the field of ultrafast spectroscopy of complex fluids and biological systems at the Universities of East Anglia and Strathclyde, he became an EPSRC Advanced Research Fellow in 2006.
In 2008, he was awarded a European Research Council Starting Investigator grant and was appointed to a Professorship in Ultrafast Chemical Physics at Strathclyde in 2016. Neil joined the University of York as Professor of Physical Chemistry in July 2018.
Research
Overview
Coherent Multidimensional Spectroscopy conference
We are delighted to be hosting the Coherent Multidimensional Spectroscopy conference (CMDS2024) at the National STEM Learning Centre, University of York from Monday 24 June to Friday 28 June 2024.
CMDS2024 will be the eleventh meeting in the series of CMDS conferences, which provides an international forum for discussion of the latest and most important results in multidimensional spectroscopy.
The meeting will bring together scientists from different fields who share the common goal of developing and implementing state-of-the-art multidimensional optical spectroscopy methods to address problems in chemistry, biology and materials science. CMDS also serves as an important venue for exchanging ideas between theorists and experimentalists. The conference will include an Early Career Symposium on Monday 24 June.
Research
Research in the NTH group uses ultrafast two-dimensional infrared (2D-IR) spectroscopy to determine the role of fast structural and solvation dynamics in biomolecular processes, ranging from ligand binding to proteins and DNA to the reactions that occur in the active sites of enzymes.
Ultrafast 2D-IR spectroscopy is the infrared equivalent of powerful multidimensional NMR spectroscopy methods in that it employs a sequence of infrared laser pulses to spread the IR absorption spectrum of a sample over a second frequency axis. The result is that the traditional IR absorption spectrum appears along the diagonal of the 2D-IR plot while the off-diagonal region contains peaks that report on couplings or energy transfer between vibrational modes. These peaks provide new information relating to molecular structure and dynamics. Combining this information with the high time resolution of 2D-IR (~ 100 fs) allows experimental visualisation of H-bond motion, dynamic conformational fluctuations of proteins or DNA. By linking ultrafast IR spectroscopy methods to lasers that can initiate a photochemical reaction or cause a fast rise in temperature of the sample we have been able to observe processes such as the melting of double stranded DNA in real time.
Examples of our work include applications of 2D-IR spectroscopy to detect the dynamics of water molecules in enzyme active sites that may play a part in their function and to understand the role of water motion in the action of synthetic catalytic systems that mimic biological molecules. We have also examined how protein structural dynamics could contribute to mechanisms of antimicrobial resistance and examined the structural and dynamical implications of ligand binding to DNA.
Recently, we have begun to explore new directions involving the application of 2D-IR to analytical problems, showing that 2D-IR can be used to analyse the protein content of biofuid samples and performing proof-of-concept 2D-IR screening experiments acquiring >2000 2D-IR spectra of DNA-ligand complexes and categorising them using novel data analysis tools.
NTH collaborates closely with scientists at STFC Rutherford Appleton Laboratory’s (RAL) Central Laser Facility and this has led to the development of 2D-IR instruments on three different RAL spectrometers that are available to the wider UK research community.
Projects
PhD projects are available in the NTH group. For more information contact neil.hunt@york.ac.uk or chemgrad@york.ac.uk.
Publications
Selected publications
2D-Infrared Spectroscopy of Proteins in Water: Using the Solvent Thermal Response as an Internal Standard
Hume, Samantha; Greetham, Gregory M.; Donaldson, Paul. M; Towrie, Michael; Parker, Anthony W.; Baker, Matthew J.; Hunt, Neil T.,. Analytical Chemistry, Vol 92, pp. 3463-3469 https://pubs.acs.org/doi/10.1021/acs.analchem.9b05601
Two-dimensional infrared spectroscopy: an emerging analytical tool?
Fritzsch, Robby; Hume, Samantha; Minnes, Lucy; Baker, Matthew J.; Burley, Glenn A.; Hunt, Neil T., Analyst Vol 145, pp. 2014-2024. https://doi.org/10.1039/C9AN02035G
Measuring proteins in H2O with 2D-IR spectroscopy.
Hume, Samantha; Hithell, Gordon; Greetham, Gregory M.; Donaldson, Paul M.; Towrie, Michael; Parker, Anthony W.; Baker, Matthew J.; Hunt, Neil T., Chemical Science Vol 10, pp. 6448-6456. https://doi.org/10.1039/C9SC01590F
Understanding the structure and dynamics of hydrogenases by ultrafast and two-dimensional infrared spectroscopy.
Horch, Marius; Schoknecht, Janna; Wrathall, Solomon L. D.; Greetham, Gregory M.; Lenz, Oliver; Hunt, Neil T., Chemical Science Vol 10, pp. 8981-8989. (2019) https://doi.org/10.1039/C9SC02851J
Quantifying secondary structure changes in Calmodulin using 2D-IR spectroscopy
Minnes Lucy, Shaw Daniel J., Cossins Benjamin P., Donaldson Paul M., Greetham Gregory M., Towrie Michael, Parker Anthony W., Baker Matthew J., Henry Alistair J., Taylor Richard J., Hunt Neil T. Analytical Chemistry Vol 89, pp. 10898- 10906(2017) http://dx.doi.org/10.1021/acs.analchem.7b02610
Examining the role of protein structural dynamics in drug resistance in Mycobacterium tuberculosis
Shaw Daniel J., Hill Rachel E., Simpson Niall, Husseini Fouad S., Robb Kirsty, Greetham Gregory M., Towrie Michael, Parker Anthony W., Robinson David , Hirst Jonathan D. , Hoskisson Paul, Hunt Neil T. Chemical Science (2017) http://dx.doi.org/10.1039/C7SC03336B
Disruption of key NADH-binding pocket residues of the Mycobacterium tuberculosis InhA affects DD-CoA binding ability
Shaw Daniel J., Robb Kirsty, Vetter Beatrice V., Tong Madeline, Molle Virginie, Hunt Neil T., Hoskisson Paul A. Scientific Reports Vol 7, (2017) http://dx.doi.org/10.1038/s41598-017-05042-4
Ultrafast 2D-IR and optical Kerr effect spectroscopy reveal the impact of duplex melting on the structural dynamics of DNA
Hithell Gordon, González-Jiménez Mario, Greetham Gregory M., Donaldson Paul M., Towrie Michael, Parker Anthony W., Burley Glenn A., Wynne Klaas, Hunt Neil Physical Chemistry Chemical Physics, (2017)
2D-IR spectroscopy shows that optimised DNA minor groove binding of Hoechst33258 follows an induced fit model
Ramakers Lennart A. I., Hithell Gordon, May John J., Greetham Gregory M., Donaldson Paul M., Towrie Michael, Parker Anthony W., Burley Glenn, Hunt Neil Journal of Physical Chemistry B, (2017) http://dx.doi.org/10.1021/acs.jpcb.7b00345
Using experimental and computational energy equilibration to understand hierarchical self-assembly of Fmoc-dipeptide amphiphiles
Sasselli I.R., Pappas C. G., Matthews E., Wang T., Hunt Neil, Ulijn Rein, Tuttle Christopher Soft Matter Vol 2016, pp. 8307-8315, (2016)http://dx.doi.org/10.1039/c6sm01737a
