The Centre for Molecular and Structural Biochemistry is a multidisciplinary biomolecular research centre based in UEA's Schools of Chemistry, Biological Sciences and Pharmacy. 

Scientists work at the interface between biology and chemistry in an environment that enables complementary expertises to be applied to important biological problems. Prof Nick Le Brun has been Director of the Centre since 2010.

OUR HISTORY

Launched in the late 1980s by Andrew Thomson FRS OBE and Colin Greenwood, the Centre for Metalloprotein Spectroscopy and Biology provided an umbrella for a range of successful interactions between UEA chemists and biologists that aimed to solve a range of significant biological problems. The Centre, which was the forerunner of the many interdisciplinary research centres that have sprung up in recent years, built an international reputation for excellence in research and pioneering innovative techniques.

As its name suggests, the focus of the CMSB was metalloproteins - proteins that contain metals, which are essential for many key cellular processes. In particular, our work focused on the activation and redox cycling of inorganic substrates involved in bacterial nitrogen, oxygen and sulphur cycles, and on metal ion metabolism and metal-microbe interactions. See the article in Biochem. Soc. Trans. by Prof Mike Wilson for more on our history.

Though the links between chemists and biologists at UEA remain as strong as ever, the focus of their work has broadened significantly in recent years into areas including protein folding, environmental sensing, pathogen-host interactions and cancer biology. To reflect this change, a celebratory meeting headlined by the Nobel Laureate Professor Sir John Walker FRS was held in May 2008 and the Centre was renamed the Centre for Molecular and Structural Biochemistry.

Through multi-million pound investment over many years from BBSRC, the Royal Society and the Wellcome Trust, the Centre boasts a broad and unique range of biophysical facilities. These include high field NMR, pulsed multi-frequency EPR spectrometer, magnetic circular dichroism, protein film electrochemistry, mass spectrometry and rapid reaction kinetics, supported by a host of additional biophysical and bioanalytical equipment.