Dr Mark Howard

Dr Mark Howard


BSc (Hon) Chemistry in 1991 from the University of Aston in Birmingham, UK.

PhD, Chemistry in 1995 from the University of Aston in Birmingham, UK.

PGCHE in 2004 from the University of Kent

Mark's PhD was in theoretical and practical nuclear magnetic resonance (NMR) spectroscopy, specifically novel solid-state NMR methods involving ultrasound. Following his PhD Mark became a post-doctoral researcher with Prof. Richard Perham FRS in Cambridge working on NMR studies of proteins including pyruvate dehydrogenase multienzyme complex (PDHc).  Following this Mark became NMR Technical Officer at the University of Kent with Prof Robert Freedman and Dr Mark Carr before returning to Cambridge to become NMR Facility Manager for the Medical Research Council Centre for Protein Engineering (MRC CPE) under the directorship of Professor Sir Alan Fersht FRS.  Mark then worked in industry on DNP Hypersense with Amersham Pharmacea/GE Healthcare and became one of the primary named inventors on the DNP Hypersense NMR Patent before returning to the University of Kent as a NMR Facility Manager in the School of Biosciences.  At Kent, he advanced into an academic role and developed from Lecturer through to Reader with a successful research group using NMR and biophysics to study protein and peptide structure, nuclear relaxation, ligand-observe drug discovery and biological oxidation and reduction. He left Kent in 2016 to take up a senior academic post at the University of Western Australia, which also involved management of a 5 spectrometer facility. However, personal reasons led to a return to the UK and he and his family settled in West Yorkshire in 2018 where Mark now works as the Technical NMR Manager for The School of Chemistry.


  • Manager and Lechnical Lead for NMR Spectroscopy

Research interests

Mark is very interested in NMR method development to answer research questions. A particular interest is using NMR spectroscopy to study molecular dynamics through nuclear relaxation and intermolecular interactions using chemical shifts and cross-relaxation transfer methods using both target and ligand observe approaches.

Key successes include:

1) The first application of two-dimensional saturation-transfer difference NMR spectra between peptides and proteins; in our case to demonstrate interactions between a cancer target and peptide drug candidate.

2) Quantitative saturation transfer to triage drug discovery contacts and accelerate drug design.

3) Using NMR spectroscopy to measure protein reductions potentials to high precision.

4) Using both fluorine and nitrogen NMR to observe and correlate both target- and ligand- observe interaction events in a biological protein system

5) Optimising multiple NMR experiment approaches for the characterisation of macrocyclic systems

6) Peptide nuclear relaxation analysis describing motions on the microsecond to picosecond timescale infers docking affinity to a protein target

7) Targeted design of a fluorine-based fragment library for industrial drug discovery and experimental NMR optimisation for high-throughput


  • BSc Chemistry
  • PhD Chemistry

Professional memberships

  • CSCi
  • CChem
  • MRSC