To date my research work has been focused on the absolute quantification of the enzymes of the tetrapyrrole branch point in Synechocystis PCC6803. After a slow and very frustrating start I feel I am beginning to make some progress! As part of this work I had to learn to do 2D gel electrophoresis and whilst my initial attempts were rubbish I can now produce some gels which I'm really pleased with. I have also begun to successfully identify the proteins from the two membrane fractions UPB and ICM from the photosynthetic R. Sphaeroides and have found over 200 proteins so far. In the future protein turnover from the two membrane fractions will be investigated using stable-isotope labelling in conjunction with proteomics based techniques.
More recently my research work has been mainly focused on the identification of proteins from two membrane fractions, UPB and ICM, from the photosynthetic organism Rhodobacter sphaeroides. So far I have identified over 300 and now have a good overview of the differing complement of proteins between the two fractions. This particular project is almost finished and we are hoping to publish in the coming months. In addition to my work on R. sphaeroides I am also attempting to run some quantification studies on the Mg-chelatase enzyme from the photosynthetic cyanobacterium Synechocystis sp. PCC 6803. At present there is no measure of the number of each subunit of this enzyme required to make the functional complex. I presented a poster of my results at the 4th Joint BSPR/EBI Proteomics meeting in Cambridge in July 2007.