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Matt Hicks CV

Dr Matthew R. Hicks, BSc. (Hons), D.Phil. MRSC


1999    D.Phil. Protein Biochemistry. University of Sussex.

Thesis title: ‘Coiled-coil assembly by proteins and peptides with unusual sequence motifs’.

1995    B.Sc.(Hons) Biochemistry. University of Bristol.

Including courses in Chemistry (Organic, Inorganic and Physical), Molecular Genetics, Microbiology and Pathology.

1991    Advanced Level: Biology, Chemistry, Mathematics, Physics.

Positions Held

2005-present University of Warwick. Senior Research Fellow

As well as continuing the research from my Wellcome fellowship, key activities include liaising with companies (both multinational and SMEs), in order to commercialise technologies and methodologies developed in our laboratory. In addition to this I supervise PhD, masters and undergraduate students in the laboratory and initiate and maintain collaborations both nationally and internationally. Other areas of activity include writing applications for funding and articles for publication in peer-reviewed journals and some undergraduate/masters teaching.

2004-2005 University of Warwick. Wellcome VIP Research Fellow

The research initiated during this fellowship, at the interface between biology and chemistry, is concerned with using spectroscopic techniques to elucidate the orientation of subunits within biological polymers. In particular, the use of linear dichroism and other biophysical techniques to investigate DNA-protein/drug interactions, protein fibres and membrane proteins.

2002-2004 University of Warwick. Research Fellow.

This project involved the production of a synthetic glycosylphosphatidyl-inositol mimetic in order to anchor recombinant prion protein to model membranes. We investigated structural and dynamic effects of anchoring the protein in membranes, using a variety of biophysical techniques and working in ClassIII containment conditions.

1999-2002 University of Sussex. Research Fellow.

This project involved the design of peptide-based anti-viral agents. A synthetic peptide was successfully used to block the dimerisation and subsequent DNA binding of the immediate-early transcription factor BZLF1 (from Epstein-Barr virus).

1996-1999 University of Sussex. Undergraduate Teaching.

I enjoy teaching and took several tutorial groups throughout my time at Sussex. In addition to this I supervised laboratory classes with responsibility for the safety of students. I have given undergraduate lectures.

1995 University of Bristol. Research Assistant.

I was working as part of a multi-discipline venture called the Molecular Recognition Centre. This involved collaboration between several faculties and served to develop my skills in working with scientists and administrators from a wide background.

Other relevant experience


A team player

Patent application preparation

Product development and commercialisation

Consultancy (method development)

Securing research funding

Preparation of manuscripts and reports to a high standard

Independent working and lateral thinking

Diverse research experience across biological, chemical and medical fields

Set-up and organisation of seminar series and other events

Competent and comfortable presenting work to a wide range of audiences


Linear and circular dichroism spectroscopy

Fourier transform infra-red spectrometry (transmission and ATR)

Dynamic light scattering

Fluorescence spectroscopy techniques

Analytical ultracentrifugation

Surface plasmon resonance (Biacore)

HPLC and FPLC (reverse-phase, SEC, ion-exchange etc, analytical and preparative)

Molecular biology (PCR, sub-cloning and site-directed mutagenesis)

Recombinant protein expression and purification

Class III containment working

Gel electrophoresis (band-shift, IEF, sequencing and SDS-PAGE)

Electron microscopy sample preparation (negative stain and cryo)

Peptide synthesis

Basic programming skills

Member of the Royal Society of Chemistry

Chair of the Biophysical Chemistry Interest Group

Member of the Biochemical Society

Visiting Researcher at Birmingham University

Peer Reviewed Publications

(1) Hicks, M. R., Halsall, D. J., Vladimirou, E., Rodger, A., and Dafforn, T. R. (2008) Real-Time PCR Detected Using Linear Dichroism Spectroscopy. In preparation for Nucleic Acids Research.

(2) Oates, J., Hicks, M. R., Dafforn, T. R., DiMaio, D., and Dixon, A. M. (2008) Role of the Transmembrane Domain in Stable Dimerization of the Bovine Papillomavirus E5 Protein. Submitted to JBC.

(3) Hicks, M. R., Dafforn, T. R., and Rodger, A. (2008) Insertion of the Peptide Antibiotic Gramicidin D into Membranes: Screening Using Linear Dichroism Spectroscopy. JMB.

(4) Hicks, M. R., Rullay, A. K., Pedrido, R., Crout, D. H., and Pinheiro, T. J. (2008) Efficient synthesis of methanesulphonate-derivated lipid chains for attachment of proteins to lipid membranes. Submitted to Synthetic Communications.

(5) Hicks, M. R., Conner, M., Dafforn, T. R., Knowles, T. J., Ludwig, C., Overduin, M., Gunther, U. L., Thome, J., Wheatley, M., Poyner, D. R., and Conner, A. C. (2008) The C-terminus of a family B G-protein coupled receptor has a structurally defined eighth helix involved in cellular trafficking and a distal internalization domain. Submitted to Biochemistry.

(6) Damianoglou, A., Scott, P., Crust, E., Ravi, J., Hicks, M. R., Knight, A., and Rodger, A. (2008) A new reference material for circular dichroism. Chirality (In Press).

(7) McDonnell, U., Kerchoffs, J. M. C. A., Castineiras, R. P. M., Hicks, M. R., Hotze, A. C. G., Hannon, M. J., and Rodger, A. (2008) Synthesis and cytotoxicity of dinuclear complexes containing ruthenium(II) bipyridyl units linked by a bis(pyridylimine) ligand. Dalton Trans 5, 667-675.

(8) Hicks, M. R., Gill, A. C., Bath, I. K., Rullay, A. K., Sylvester, I. D., Crout, D. H., and Pinheiro, T. J. (2006) Synthesis and structural characterization of a mimetic membrane-anchored prion protein. Febs J 273, 1285-99 (and Front Cover).

(9) Hicks, M. R., Rodger, A., Thomas, C. M., Batt, S. M., and Dafforn, T. R. (2006) Restriction Enzyme Kinetics Monitored by UV Linear Dichroism. Biochemistry 45, 8912-7.

(10) Rajendra, J., Damianoglou, A., Hicks, M., Booth, P., Rodger, P. M., and Rodger, A. (2006) Quantitation of protein orientation in flow-oriented unilamellar liposomes by linear dichroism. Chemical Physics 326, 210-220.

(11) Rodger, A., Marrington, R., Geeves, M. A., Hicks, M., de Alwis, L., Halsall, D. J., and Dafforn, T. R. (2006) Looking at long molecules in solution: what happens when they are subjected to Couette flow? Physical Chemistry Chemical Physics 8, 3161-3171.

(12) Marrington, R., Dafforn, T. R., Halsall, D. J., MacDonald, J. I., Hicks, M., and Rodger, A. (2005) Validation of new microvolume Couette flow linear dichroism cells. Analyst 130, 1608-16.

(13) Schelcher, C., Valencia, S., Delecluse, H. J., Hicks, M., and Sinclair, A. J. (2005) Mutation of a single amino acid residue in the basic region of the Epstein-Barr virus (EBV) lytic cycle switch protein Zta (BZLF1) prevents reactivation of EBV from latency. J Virol 79, 13822-8.

(14) Hicks, M. R., Al-Mehairi, S. S., and Sinclair, A. J. (2003) The zipper region of Epstein-Barr virus bZIP transcription factor Zta is necessary but not sufficient to direct DNA binding. J Virol 77, 8173-7.

(15) Hicks, M. R., Walshaw, J., and Woolfson, D. N. (2002) Investigating the tolerance of coiled-coil peptides to nonheptad sequence inserts. J Struct Biol 137, 73-81.

(16) Offer, G., Hicks, M. R., and Woolfson, D. N. (2002) Generalized Crick equations for modeling noncanonical coiled coils. J Struct Biol 137, 41-53.

(17) Hicks, M. R., Balesaria, S., Medina-Palazon, C., Pandya, M. J., Woolfson, D. N., and Sinclair, A. J. (2001) Biophysical analysis of natural variants of the multimerization region of Epstein-Barr virus lytic-switch protein BZLF1. J Virol 75, 5381-4.

(18) Hicks, M. R. (2000) Coiled-coil assembly by proteins and peptides with unusual sequence motifs. D.Phil. thesis.

(19) Hicks, M. R., Holberton, D. V., Kowalczyk, C., and Woolfson, D. N. (1997) Coiled-coil assembly by peptides with non-heptad sequence motifs. Fold Des (and Front Cover) 2, 149-58.