Molecular Biophysics lies at the intersection of Physics, Chemistry and Biology. It employs techniques and technologies from each discipline to understand the biological world in terms of the fundamental molecules that comprise it. Molecular Biophysics and Enzymology are closely associated with the fields of Molecular Biology and Biochemistry.
Our Molecular Biophysics research aims to understand the composition and function of biomolecules such as DNA, RNA and proteins – the fundamental molecules that control all life. By understanding how biomolecules are made and function, we're finding new ways to modify and manipulate their behaviour, so they can have societally, industrially and medically useful functions such as in biofuels, manufacturing, cleaning up pollution and providing effective medicines.
Our research is already making an impact. We're finding solutions to some of the major problems facing society and the planet – from combatting plastic pollution, to developing new drug treatments for human diseases.
Our research employs approaches from the following fields
- Structural biology
- Physical biochemistry
- Synthetic biology
- Molecular biology
- Molecular enzymology
We have facilities for X-ray crystallography and Nuclear Magnetic Resonance (NMR), which we use to study the shape, structure and dynamics of biomolecules. We also house analytical ultracentrifugation (AUC) and surface plasmon resonance (SPR) facilities which are key for analysing how biomolecules interact with each other.
Once we understand the natural structure and function of a biomolecule, such as a protein or RNA, we use molecular engineering and molecular biology techniques to modify its structure and therefore its function – providing solutions to societal, biomedical and industrial problems.
Research collaboration and funding
We regularly collaborate on research with industry and academic partners around the world. We work on projects with Diamond Light Source (the UK centre for Biophysical research), the National Renewable Energy Laboratory (NREL), STORM Therapeutics Ltd, the Mary Rose Trust, and GlaxoSmithKline plc. We're also an active part of the Proteomics Consortium (S4PC) with the University of Southampton, the University of Surrey and the University of Reading.
We've received research funding from major funders such as the Biotechnology and Biological Sciences Research Council (BBSRC), the Defence Science and Technology Laboratory (DSTL), the National Renewable Energy Laboratory, USA (NREL) and Innovate UK, a non-departmental public body that serves as the UK's innovation agency.
Publications and coverage
Our research frequently makes headlines in the press and is featured in major scientific publications, such as Nucleic Acids Research, the Journal of Molecular Biology, Journal of Biological Chemistry, and Proceedings of the National Academy of Sciences, Genes and Development.
The discovery of a 'plastic-eating' enzyme by Professor John McGeehan and his team and Dr Garry Scarlett's and Dr Sam Robson’s research identifying members of the Mary Rose through the study of their DNA, achieved global coverage from major media organisations including the Guardian, the BBC, Al Jazeera, CNN and Reuters.
Centre for Enzyme Innovation
At the Centre for Enzyme Innovation, we're researching solutions to some of the most pressing global environmental problems. We're learning from the natural world – working to deliver transformative enzyme-enabled solutions for circular recycling of plastics.
We were recently awarded £5.8 million from the Research England Expanding Excellence Fund. Coupled with significant investment by the University, this major funding will speed up our progress towards finding a solution to one of the world’s greatest environmental challenges – plastic waste.
Find out more about the work we're doing at the Centre – and read all about our major funding news – below.
Proc Natl Acad Sci U S A (2018), 115(19), E4350-E4357, doi: 10.1073/pnas.1718804115: H.P. Austin, M.D. Allen, B.S. Donohoe, N.A. Rorrer, F.L. Kearns, R.L. Silveira, B.C. Pollard, G. Dominick, R. Duman, K. El Omari, V. Mykhaylyk, A. Wagner, W.E. Michener, A. Amore, M.S. Skaf, M.F. Crowley, A.W. Thorne, C.W. Johnson, H.L. Woodcock, J.E. McGeehan, G.T. Beckham
Nucleic Acids Res. (2018), 46(14):e86. doi: 10.1093/nar/gky410: J.O. Phillips, L.E. Butt, C.A. Henderson, M. Devonshire, J. Healy, S.J. Conway, N. Locker, A.R. Pickford, H.A. Vincent, A.J. Callaghan
ACS Synth Biol. 2019 Feb 15;8(2):207-215. doi: 10.1021/acssynbio.8b00266.Norouzi M, Pickford AR, Butt LE, Vincent HA, Callaghan AJ.
7 glycoside hydrolase (GH) enzyme
Professor John McGeehan solved the X-ray crystal structure of a novel family 7 glycoside hydrolase (GH) enzyme. Biophysical and biochemical data show that this enzyme is highly salt tolerant with novel features that make it attractive from an industrial biofuels perspective.
Novel approaches to targeting antibiotic resistance
With antibiotic resistance on the rise, research into understanding the workings of bacterial organisms is crucially important, as are new approaches to combating the infections they cause. Professor Callaghan and Dr Gowers, together with colleagues at the University of Leeds, Imperial College London, the University of Viscosa and DSTL, are working to address this topical and strategically relevant issue. A range of approaches are being explored; from targeting essential enzymes found in pathogenic bacteria, to targeting molecular switches responsible for turning on bacteria virulence.
Professor McGeehan and researchers at the U.S. Department of Energy's National Renewable Energy Laboratory and the University of South Florida, solved the high-resolution structure of the PETase enzyme using X-ray crystallography at the Diamond Light Source. The team used the structure to design an improved version of the enzyme, making it more efficient, and raising the possibility of further efficiency gains.
Structure-function relationships in matrix metalloproteinases
Dr Pickford's group are investigating the molecular mechanisms that underpin the breakdown of collagen fibres in the articular cartilage that lines the synovial joints of the body. The gradual destruction of this tissue is a common pathological feature of the chronic inflammatory condition rheumatoid arthritis (RA). The enzymes predominantly responsible for breaking down collagen in RA are members of the matrix metalloproteinase (MMP) family. These collagen-degrading MMP enzymes are secreted by cells as inactive zymogens which are then activated in the extracellular space. The Pickford group are researching the mechanism of activation of these collagenases and the way in which they break down articular collagen.
Studying and exploiting RNA-based interactions
Professor Callaghan’s team researches RNA-based control mechanisms important in gene expression pathways. To explore the molecular interactions involved, she developed an innovative technology to support high-throughput studies and, with Dr Pickford and colleagues at the Universities of Oxford and Surrey, has completed proof-of-concept studies. Together with Dr Scarlett and colleagues at the University of Massachusetts, applications within the synthetic biology domain are presently being explored, whilst it’s utility within the RNA therapeutics field is being explored with commercial partners. The technology is the subject of a patent.
Professor Geoff Kneale
Sadly, our friend and colleague Professor Geoff Kneale passed away suddenly on 24th of June. Professor Kneale, GGK to the many people who passed through his laboratory over the years, was a driving force behind Biophysics teaching and research at Portsmouth for over 30 years. Geoff obtained his undergraduate degree in Biophysics from the University of Leeds and completed a PhD in small molecule crystallography, also at the highly respected Leeds Biophysics laboratories in 1975.
After his PhD Geoff took up a post-doctoral position within the Biophysics group at Portsmouth, then a part of the physics department, on a project involving small angle neutron scattering of nucleosomes. This began Geoff’s interest in protein-DNA interactions which remained a research focus for the rest of his career.
After Portsmouth, Geoff held post-doctoral research positions at both Cambridge, working on non-standard DNA base pairing, and EMBL where he began his research into bacteriophage Gene V proteins. In 1987, Geoff returned to the Biophysics group at Portsmouth, by this time part of the Biology department, as a member of academic staff. Notably during the late 1980s he started his work on bacterial restriction-modification systems, which provided a rich seam of study over the coming years.
Geoff was not only a successful research scientist but a highly respected teacher to both undergraduates and his many postgraduate students, explaining complex concepts in a clear, precise manner often with some humour. Geoff was at the core of the development of the science faculty at Portsmouth, leading the RAE and later REF submissions. He was instrumental in setting up and leading the very successful Institute of Biomedical and Biological Sciences (IBBS) within the faculty, which remains the vehicle for delivering research excellence in both topics at Portsmouth.
Geoff took a phased retirement and as Emeritus remained a common sight in the Biophysics tearoom and a good friend to the many students who had passed through his laboratory.
Discover our areas of expertise
Through our biodiversity and evolution research, we're expanding our knowledge of the diverse organisms that exist across the Tree of Life – from microbes to whales.
We explore new ways to treat genetic disorders, identifying novel targets for drugs and searching for advances in treatment that could impact the lives of millions.
We're examining how humans impact ecosystems, and developing new ways to assess and counteract our impact on the environment.
Through our research in marine science, we're working to improve the marine environment for future generations, and to make marine activities more sustainable.