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Facility for the kinetic analysis of protein function folding and stability

Reference	JE616389
Principal Investigator / Supervisor	Professor Andrew Trevor Smith
Co-Investigators / Co-Supervisors	Dr Benjamin Adams, Dr John Armstrong, Professor Stephen Caddick, Professor Dek Woolfson
Institution	University of Sussex
Department	Sch of Life Sciences
Funding type	Research
Value (£)	71,168
Status	Completed
Type	Research Grant
Start date	01/05/2002
End date	01/05/2003
Duration	12 months

Abstract

Rapid kinetic methods offer the potential to resolve the time-scales for protein conformational events underlying biological molecular recognition events such as protein folding, coiled-coil assembly and protein-ligand interactions. We wish to establish at Sussex a facility for the kinetic analysis of protein conformational events, specifically: (i) To compare the unfolding pathway of peroxidase enzymes from class II (fungal origin) and class III (higher plant) and the linkage between Ca2+ binding and stability by means of selected Ca2+ site mutants, and super stable mutants identified from forced evolution studies. (ii) To probe the conformational events underlying the activity of dimethyl sulphoxide reductase (DMSOR) and other molybdoproteins. (iii) To determine the association/assembly mechanism of model coiled-coil proteins and protein fibres. (iv) To probe the nature and kinetics of the interaction between the Neocarzinostatin chromophore and its chromoprotein complex. (v) To characterised the molecular event underlying complex formation between SNARE proteins and other cognate partners.

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	Joint Equipment Initiative 2001 (JE6) [2001]
Funding Scheme	X – not Funded via a specific Funding Scheme

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