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Understanding chaperone-assisted protein folding at the molecular level
Reference
B04804
Principal Investigator / Supervisor
Professor Sheena Radford
Co-Investigators /
Co-Supervisors
Institution
University of Leeds
Department
Inst of Molecular & Cellular Biology
Funding type
Research
Value (£)
129,123
Status
Completed
Type
Research Grant
Start date
01/03/1996
End date
01/03/1999
Duration
36 months
Abstract
The aim is to elucidate the molecular basis by which the molecular chaperone, GroEL, facilitates protein folding using the well characterised protein, hen lysozyme as a model for the refolding polypeptide chain. Specific questions are the relationship between the assisted and unassisted folding pathways; the nature and location of the binding sites for lysozyme on GroEL; and the conformation of intermediates bound to the chaperonin. A battery of biophysical techniques including NMR, mass spectrometry, calorimetry, surface plasmon resonance and stopped flow spectroscopy, backed up by biochemical methods, will be used to address these important questions.
Summary
unavailable
Committee
Closed Committee - Biomolecular Sciences (BMS)
Research Topics
X – not assigned to a current Research Topic
Research Priority
X – Research Priority information not available
Research Initiative
Biological Chemistry Initiative (BCI) [1995]
Funding Scheme
X – not Funded via a specific Funding Scheme
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