Synergy at the chemistry biology interface Synergy at the chemistry biology interface

Research in the Biophysical and Biological Chemistry group falls under the umbrella of the Centre for Molecular and Structural Biochemistry (CMSB), a cross-School research centre that achieves synergy through the interactions of scientists at the chemistry-biology interface. Virtually all of our projects are collaborative, involving others at UEA, or groups located nationally or internationally.  

Research is focused on the development and application of advanced biophysical techniques, including pulsed magnetic resonance (EPR and NMR) and magneto-optical spectroscopies, protein film electrochemistry and mass spectrometry, to address important questions in biology. Major projects include studies of nitrogen cycle, sulfur cycle and respiratory chain enzymes, metal ion metabolism, biological sensors, protein folding and plant-microbe interactions.  Synthetic biology, including applications in bioenergy, is a growing part of our research.

Research is currently led by the following members of Faculty:

Prof Peter Belton

Prof Peter Belton

  • Use of cereal proteins to make biodegradable plastics and as drug delivery systems.
  • Applications of spectroscopy and other physical characterisation to food and drug delivery systems

Dr Tharin Blumenschein

Dr Tharin Blumenschein

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

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.

     

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)

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

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 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

Prof Geoffrey R Moore

Prof Geoffrey R Moore

  • Natively unfolded proteins
  • Intermolecular interactions involving proteins
  • Biomolecular NMR spectroscopy

Dr Vasily Oganesyan

Dr Vasily Oganesyan

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

Prof Chris Pickett

Prof Chris Pickett

  • Artificial Hydrogenases
  • Photoelectrocatalytic devices for hydrogen generation, carbon dioxide fixation and alkane functionalisation
  • Electropolymer materials

Dr Amit Sachdeva

Dr Amit Sachdeva

 

Prof Andrew J Thomson

Prof Andrew J Thomson

  • Iron sulfur clusters as regulators of bacterial genes in response to environmental factors such as redox stress, oxygen and nitric oxide