Dr Matt Webster

Head of School - Allied Health

Faculty:Faculty of Health, Education, Medicine and Social Care

School:Allied Health

Location: Chelmsford

Areas of Expertise: Cancer biology , Pharmaceutical science

Matt has a research background in molecular biology, particularly in protein DNA interaction. He is Head of School for Allied Health but still lectures in molecular biology and acts as External Examiner for a number of UK institutions.



Matt completed his undergraduate studies at the University of Kent before moving into industry. Having worked for a number of major pharmaceutical companies in the UK, he completed his PhD at the Institute of Structural and Molecular Biology under the supervision of Dr Tracey Barrett. Using the technique of Protein Crystallography he successfully solved the structure of the DNA damage repair protein UvRB, showing it to be dimeric in damage scanning.

Following postdoctoral work at Birkbeck College, Matt secured a research fellowship with Cancer Research UK, working in the laboratory of Dr Martin Singleton and investigating the role of various Histone binding proteins in the formation of the mitotic spindle.

Matt has always had a keen passion for science education and moved to a post at Anglia Ruskin's associate college in Harlow where he led the validation and delivery of a new BSc (Hons) in BioScience. He is now the course leader for the range of extended degrees in Nutrition, Medical Science and Pharmaceutical Science.

Research interests

  • DNA repair
  • Protein crystallography
  • Student engagement and assessment strategy

Areas of research supervision

  • Molecular biology
  • Protein expression and purification
  • Student engagement and assessment strategy


  • PhD Structural Biology, University of London (UCL/Birkbeck)
  • BSc (Hons) Biomedical Science, University of Kent at Canterbury
  • Diploma in Education, Acentis

Selected recent publications

Webster, M.P., Jukes, R., Zamfir, V.S., Kay, C.W., Bagnéris, C. and Barrett T., 2012. Crystal structure of the UvrB dimer: insights into the nature and functioning of the UvrAB damage engagement and UvrB-DNA complexes. Nucleic Acids Research, 17(40), pp.8743-58