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Conformational dynamics and catalysis of aldolase studied by NMR spectroscopy

Reference	BBS/B/05680
Principal Investigator / Supervisor	Professor Alan Berry
Co-Investigators / Co-Supervisors	Professor Steve Homans
Institution	University of Leeds
Department	Inst of Molecular & Cellular Biology
Funding type	Research
Value (£)	207,944
Status	Completed
Type	Research Grant
Start date	26/07/2004
End date	25/07/2007
Duration	36 months

Abstract

Proteins are not static, and conformational changes play vital roles in enzyme catalysis, with motions ranging both in scale and frequency. Moreover, transient structural rearrangements may preferentially stabilise the transition state and there is now compelling evidence that conformational dynamics govern the rate of catalysis. Here, we will use modern NMR relaxation techniques to probe the dynamics of fructose bisphosphate aldolase at each stage of its catalytic cycle to full delineate the role of motions on catalysis, enabling further insights into the workings of this important enzyme in the context of enzyme re-design and evolution. The work will also demonstrate the feasibility of this approach on large enzymes and proteins.

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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