Chemistry of Life Processes Chemistry of Life Processes

Research under the Chemistry of Life Processes theme applies state of the art technologies in areas such as biophysical chemistry, theoretical simulation, protein engineering and genetic programming to understand a wide range of biological processes and to develop synthetic biology approaches towards novel applications of biological systems. Systems under study include the roles of metals in life, nitrogen cycle enzymes, multiheme cytochromes, membrane transporters, protein-protein interactions and unnatural amino acids.

Prof Julea N. Butt

Prof Julea N. Butt

  • Multi-heme cytochromes of Shewanella oneidensis MR-1
  • Voltammetric and spectroelectrochemical studies of redox-active metalloproteins.
  • Biophysical characterisation of enzymes catalysing the biogeochemical cycling of nitrogen, sulphur and iron.

     

Prof Nick E Le Brun

Dr Nick E Le Brun

  • Mechanisms of iron storage in single cell organisms
  • Copper trafficking in bacterial cells
  • Sensing of oxidative and nitrosative stress by iron-sulfur cluster containing transcriptional regulators

Dr Andrew M Hemmings

Dr Andrew M Hemmings

  • X-ray structural and mechanistic studies of enzymes
  • Enzyme engineering
  • Metal-protein recognition and the role of metals in Biology
  • Computational structural biology

Dr Vasily Oganesyan

Dr Vasily Oganesyan

  • Theoretical and Computational methods for advanced spectroscopy
  • Electronic structure calculations
  • Molecular Dynamics simulations

Dr Amit Sachdeva

Dr Amit Sachdeva

  • Genetic encoding of unnatural amino acids in live cells
  • Modulating properties of antibodies using unnatural amino acids
  • Developing new synthetic biology tools for genetic code expansion in E.coli

Dr Myles Cheesman

Dr Myles Cheesman

  • EPR (electron paramagnetic resonance) and MCD (magnetic circular dichroism) spectroscopy of transition-metal centres in proteins.
  • Multi-heme enzymes involved in bacterial denitrification.
  • MOTTLE (MCD monitored optically transparent thin layer electrodes)

Prof Steve R. Meech 

Prof Steve R. Meech 

  • Ultrafast Spectroscopy
  • Photodynamics of proteins
  • Dynamics of complex fluids

Dr Fraser MacMillan

Dr Fraser MacMillan

  • Application and development of EPR (ESR) including multi-frequency, pulsed and double resonance techniques.
  • Structure/function/dynamics relationships in biomacromolecules, especially in membrane and metallo-proteins.
  • Protein - ligand interactions, electron transfer and biological transport processes.
  • Spin Labelling, EPR and distance measurements

Dr Tharin Blumenschein

Dr Tharin Blumenschein

  • Protein interactions in cancer
  • Nuclear magnetic resonance of proteins
  • Protein dynamics, interactions, and function
  • Intrinsically disordered proteins

Prof Mark Searcey

Prof Mark Searcey

  • Inhibition of protein-DNA and protein-protein interactions
  • Targeting nucleic acids and DNA repair and proliferation
  • Solution and solid phase natural product synthesis