The University of Sheffield
Department of Molecular Biology and Biotechnology

Krebs Institute Sequencing and Synthesis Facility


Dr A J G Moir
blank space The facility provides protein sequencing, peptide synthesis, DNA synthesis and DNA sequencing services for members of the Departments of Molecular Biology and Chemistry, and for staff from various departments within the Medical School. Work is also undertaken for other universities. The current value of the equipment is approx £500,000 and the annual turnover is around £50,000. Funding for the purchase of a Mass Spectrometer has recently been awarded and will expand the ability of the facility to provide a complete proteomics service. Work carried out by the Facility underpins many publications from the Department.

 

Molecular basis for the activity of AMP Deaminase from skeletal muscle : Research led by Prof A. Raggi at the University of Pisa (Italy) is determining the role of AMP deaminase in muscle tissue by investigating the molecular architecture of the protein and its interaction with zinc and a histidine-proline-rich glycoprotein that we have recently shown to be a component of the enzyme.

 

Characterisation of an aspartic protease and its application to wound healing : Research led by Prof E. Pires at the University in Coimbra and Prof M. Barros at Viseu (Portugal) into a plant protease with potential activity in minimising the formation of post-operative adhesions.

 

Characterisation of novel antibiotics A potential novel antibiotic isolated by Prof S. Mendo (Aveiro, Portugal) has been successfully characterised.

 

Selected Publications

[1] A Calpain-like proteolytic activity produces the limited cleavage at the N-terminal regulatory domain of rabbit skeletal muscle AMP deaminase. Martini, D., Montali, U. Ranier-Raggi, M., Sabbatini, A.R.M., Thorpe, S.J., Moir, A.J.G. & Raggi, A. (2204) BBA - in press
[2] Purification and characteristaion of a new peptide antibiotic produced by a thermotolerant Bacillus licheniformis strain. Mendo, S., Faustino, N.A., Sramento, A.C., Amado, F. & Moir A.J.G. (2004) Biotechnology Letts. 26, 115-119.
[3] Identification of proteins in the exosporium of Bacillus anthracis. Redmond, C., Baillie, L.W.G., Hibbs, S., Moir, A.J.G. & Moir, A. (2004). Microbiology 150, 355-363.
[4] Characterisation of the Zn-binding site of the histidine-proline-rich glycoprotein associated with rabbit skeletal muscle AMP deaminase. Mangani, S., Meyer-Klaucke, W., Moir, A.J.G., Ranieri-Raggi, M, Martini, D., & Raggi, A. (2003) J. Biol. Chem. 278, 3176-3184.
[5] Isolation by zinc-affinity chromatography of the hsitidine-proline-rich glycoprotein molecule associated with rabbit skeletal muscle AMP deaminase. Ranieri-Raggi, M. Martini, D., Sabbatini, A.R.M., Moir, A.J.G. & Raggi, A. (2003). BBA 1645, 81-88