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Structural basis of the polypeptide-binding and chaperone activities of protein disulphide isomerase

Reference	MOL04536
Principal Investigator / Supervisor	Professor Robert Freedman
Co-Investigators / Co-Supervisors
Institution	University of Kent
Department	University of Kent Department
Funding type	Research
Value (£)	145,278
Status	Completed
Type	Research Grant
Start date	01/08/1995
End date	01/01/1999
Duration	41 months

Abstract

We aim to understand the structural basis of the interaction between unfolded and partly- folded polypeptide substrates and protein disulphide-isomerase (PDI), a molecular chaperone and catalyst of protein folding. The roles of non-active-site domains of PDI will be probed and the sites of interaction between PDI and peptides and other ligands will be established by chemical labelling methods. Interactions between PDI and polypeptide substrates will be probed during both cotranslational folding and in vitro refolding. The aim is to extend understanding of the molecular basis of the action of this key facilitator of protein folding.

Summary

unavailable

Committee	Closed Committee - Biochemistry & Cell Biology (BCB)
Research Topics	X – not assigned to a current Research Topic
Research Priority	X – Research Priority information not available
Research Initiative	Molecules (Ropa) (MOL) [1994]
Funding Scheme	X – not Funded via a specific Funding Scheme

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