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|Title:||Molecular cloning, expression, purification and characterization of a recombinant FKBP family member from Pseudomonas aeruginosa.||Authors:||Tay, Shawn Wei Liang.||Keywords:||DRNTU::Science::Biological sciences::Biochemistry||Issue Date:||2010||Abstract:||The FK-506 binding proteins (FKBPs) are a family of proteins with characterised molecular functions such as peptidylprolyl cis-trans isomerase activity and chaperone activity. However, the FKBP family member from Pseudomonas aeruginosa is currently uncharacterised. This study has successfully developed a recombinant method of overexpressing and purifying the FK-506 binding domain of P. aeruginosa (PaFKBD) in a SUMO-PaFKBD fusion protein state. The characterisation of SUMO-PaFKBD revealed peptidylprolyl cis-trans isomerase activity with catalytic efficiency of 1.01 x 105 s-1 M-1 and this activity is inhibited by FK-506 with an IC50 of 92.6nM. More studies need to be done to further reaffirm these results and to further characterise the protein.||URI:||http://hdl.handle.net/10356/39981||Rights:||Nanyang Technological University||Fulltext Permission:||restricted||Fulltext Availability:||With Fulltext|
|Appears in Collections:||SBS Student Reports (FYP/IA/PA/PI)|
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