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Proteomic analysis of the Hsp90 chaperone system
Reference
C13023
Principal Investigator / Supervisor
Professor Peter William Piper
Co-Investigators /
Co-Supervisors
Institution
University College London
Department
Structural Molecular Biology
Funding type
Research
Value (£)
217,712
Status
Completed
Type
Research Grant
Start date
01/10/2000
End date
01/10/2003
Duration
36 months
Abstract
The Hsp90 chaperone system catalyses the final activation step of many important eukaryotic regulatory proteins. This project seeks to apply newly-developed proteomic techniques, based on the yeast two hybrid system, to the identification of protein-protein interactions within the several multiprotein complexes that involve Hsp90. We will determine if these procedures can be used to identify unknown targets of Hsp90; also to reveal to Hsp90 interacts with domains of the different cochaperone proteins that assist its chaperone function. These cochaperones include several proteins that contain tetratricopeptide (TPR) repeat motifs.
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
X - not in an Initiative
Funding Scheme
X – not Funded via a specific Funding Scheme
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