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Towards an understanding of the molecular basis of thermal stability from studies on glutamate dehydrogenase

Reference	C10387
Principal Investigator / Supervisor	Professor David Rice
Co-Investigators / Co-Supervisors
Institution	University of Sheffield
Department	Molecular Biology and Biotechnology
Funding type	Research
Value (£)	170,736
Status	Completed
Type	Research Grant
Start date	01/04/1999
End date	01/04/2002
Duration	36 months

Abstract

The analysis of the sequences, properties and structures of the enzyme glutamate dehydrogenase from organisms that span the known spectrum of temperature stability from pyschrophiles have led to this enzyme being adopted as a model system for the analysis of protein stability. Structural studies on the GluDHs from hyperthermophilic organisms have indicated the presence of extensive networks of ion pairs which are not found in the equivalent mesophilic enzymes. This has led to the suggestion that such networks play a key role in generating enzyme stability at high temperatures. Mutagenesis of residues involved in ion pair formation has led to significant changes in stability. The purpose of this proposal is to analyse at the level of 3D structure the results of mutagenic programmes in order to understand at the molecular level how these substitutions exert their effect.

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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