The MIB Biophysics Facility contains state-of-the-art facilities in advanced spectroscopy and kinetic techniques. We offer a range of biophysical techniques with many applications:

  • Enzyme assays: from development through to high-throughput capabilities
  • Rates of individual steps in catalysis
  • Understanding reaction mechanisms
  • Identifying new reaction intermediates
  • Optimising reaction conditions
  • Inhibitor studies
  • Ligand binding assays
  • Protein-protein interactions
  • Anaerobic reactions
  • Identifying rate-limiting steps in a reaction
  • Redox chemistry
  • Plus many more


Dr Derren Heyes | | Tel: +44(0)161 306 5159


The MIB Biophysics Facility is one of the largest, academic ‘Kinetics and Spectroscopy’ facilities for bioscience research in the world and consists of over £1.5 million of state-of-the-art instrumentation. We offer cutting-edge biophysical equipment, which can be used to study many different chemical and biological processes over a range of timescales and temperatures. The facility is actively involved in a wide range of research topics and has contributed to a number of publications in a broad range of high impact journals.

Services and equipment

We offer a very flexible and tailored usage of our facilities, ranging from a walk-in service to formal collaborations – please contact Derren to discuss your personal experimental requirements. We provide full training for new users to ensure safe and proper use of the following instrumentation:

Advance spectroscopic techniques

We have developed the use of advanced spectroscopic tools to study catalytic, binding, structural and dynamical processes in biological macromolecules:

  • Advanced fluorescence techniques. Fluorescence lifetime measurements, fluorescence resonance energy transfer (FRET) and fluorescence anisotropy to probe many molecular processes (e.g. protein-protein interactions, ligand binding, conformational changes).
  • Circular Dichroism (CD) spectroscopy. Provides important information about protein secondary structure.
  • Electrochemical approaches. Probe redox properties of biological molecules using potentiometry apparatus.
  • Fourier Transform Infra-Red (FTIR) spectroscopy. Vibrational spectroscopy technique to probe the structure and dynamics of biological molecules. FTIR is coupled to a stopped-flow device to facilitate time-resolved measurements.
  • Isothermal titration calorimetry (ITC). Thermodynamic technique for studying binding of ligands (e.g. substrates, inhibitors, DNA, RNA and other proteins) to proteins.
  • Surface plasmon resonance (SPR). SPR instruments, including Biacore, for studying a range of biomolecular interactions by measuring changes in refractive index at the sensor chip surface.

Complementary spectroscopic techniques are available in MIB in EPR spectroscopy (Steve Rigby) and Raman spectroscopy (Ewan Blanch/Roy Goodacre/Peter Gardner).

Kinetic techniques

Many chemical and biological processes occur over a range of different timescales – from femtoseconds (10-15 s) through to minutes. We offer a number of kinetic instruments to study biological and chemical reactions on the fs – sec timescale. These are used to understand reaction mechanisms, measure rates of ligand binding/catalysis and to characterise reaction intermediates.

  • Stopped flow spectroscopy. Rapid mixing kinetics technique to follow reactions on a millisecond timescale. The facility has several highly specialised stopped-flows:
    • High pressures (
    • Cryogenic temperatures (>-90°C)
    • Presence of magnetic fields
    • Stopped flow infra-red instrument to follow vibrational changes in the infra-red region
    • Freeze-quench instrument for EPR analysis
  • Temperature jump spectroscopy. Temperature perturbation technique to follow reactions on µs timescale.

Laser photoexcitation techniques

We have developed laser-based techniques in the facility to study light activated reactions on fs-sec timescale. Potential applications include light-activated enzymes and photoreceptors, photoexcitable electron donors (e.g NAD(P)H, Ru compounds, etc) and ‘caged’ compounds (e.g. caged ATP, caged O2, caged metals, etc). We have the following laser-based techniques:

  • ns laser flash photolysis
  • Laser flash photolysis coupled to high pressures and magnetic fields
  • Ultrafast pump-probe absorption spectroscopy
  • Laser-induced IR measurements (access to Central Laser Facility)
  • Laser-induced EPR spectroscopy (Steve Rigby)

We also have a large suite of anaerobic facilities, allowing all experiments to be carried out in O2-free environment.

“Over the last few years we have had a number of very successful projects in the MIB Biophysics facility using laser photoexcitation, stopped-flow and redox measurements to study different metalloenzymes. These fast kinetic studies have been a crucial tool in our understanding of how these redox enzymes work. The experiments have resulted in several important publications and will hopefully lead to many more in the coming years. This is a very good example of the close collaboration between teams from Manchester and Liverpool in the same way as Lawrence Bragg and Beevers and Lipson in X-ray Crystallography.”

Professor Samar Hasnain, University of Liverpool

“We have used the MIB Biophysics facility on a number of occasions to study the mechanism of a novel cytochrome P450 enzyme. The kinetic instrumentation and anaerobic capabilities are excellent and the expertise provided has been invaluable for our studies. We look forward to continued use of the facility in the future.”

Dr Sarah Barry, Kings College, London