Full name: 
Ms. Tracy Keates

Affiliation

Structural Genomics Consortium, University of Oxford
Research interests: 

The University of Oxford is a complex and stimulating organisation, which enjoys an international reputation as a world-class centre of excellence in research and teaching. It employs over 10,000 staff and has a student population of over 21,000. The Structural Genomics Consortium (SGC) is a not-for-profit, public-private partnership that conducts pre-competitive research to facilitate the discovery of new medicines. Based at the University of Oxford and University of Toronto the SGC's work contributes to new hypotheses in understanding and treating human disease, and the subsequent identification of new targets for drug discovery. The SGC’s primary objectives are to produce and characterise the 3-dimensional structures of soluble proteins and of integral membrane proteins, to generate selective chemical probes for epigenetic proteins and kinases, and to release these into the public domain. As part of its mission the SGC generates medically relevant reagents and knowledge related to human proteins and proteins from human parasites, which it shares through over 250 collaborations with researchers worldwide. Since 2004 the SGC has solved over 1300 protein structures, generated 8 inhibitors of epigenetic proteins, and regularly contributed articles to leading publications including Nature and Science.

Content published on MolMeth

Biotinylation of an antigen is often the method of choice for protein immobilization to select and evaluate affinity reagents. The tight and specific interaction of biotin with streptavidin or avidin is thereby used in many selection systems to specifically capture the antigen and/or affinity reagent for further analysis. In vitro biotinylation is frequently used, whereby lysine residues in the antigen are chemically modified. Biotinylation of a short acceptor peptide in vivo is an attractive method to achieve site-specific modification without the risk to interfere with protein folding or function of the antigen. In vivo biotinylation is achieved by co-expressing the protein of choice (fused to a biotin acceptor peptide) and the bacterial biotin-protein ligase, holocarboxylase synthetase (BirA) in the presence of biotin.