Award details

Conformational properties of unfolded states and folding intermediates of Im proteins determined by NMR

Reference	B18663
Principal Investigator / Supervisor	Professor Geoffrey Robert Moore
Co-Investigators / Co-Supervisors	Professor Sheena Radford
Institution	University of East Anglia
Department	Chemistry
Funding type	Research
Value (£)	195,176
Status	Completed
Type	Research Grant
Start date	01/05/2003
End date	30/04/2006
Duration	36 months

Abstract

The family of 9.5 kDa Im proteins are a good model system for delineating protein folding mechanisms: some fold in a 2-state transition and others in a 3-state transition via an intermediate. NMR will be used to determine the structures of intermediates and the ordering and dynamics of the unfolded forms, thereby providing a structural perspective on Im folding. Urea-unfolded native Ims will be studied, as will mutant Ims that resemble stabilised unfolded and intermediate forms in the absence of denaturant. The roles of aromatic groups in ordering unfolded Im will be studied with mutants. NMR methods will include multinuclear experiments to measure NOEs, residual dipolar couplings, 15N relaxation parameters, and diffusion coefficients.

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	X - not in an Initiative
Funding Scheme	X – not Funded via a specific Funding Scheme

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