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Guided evolution of new dehydrogenase catalysts: phage display and plate screens

Reference	B05296
Principal Investigator / Supervisor	Professor John Holbrook
Co-Investigators / Co-Supervisors
Institution	University of Bristol
Department	Biochemistry
Funding type	Research
Value (£)	163,516
Status	Completed
Type	Research Grant
Start date	01/10/1995
End date	01/12/1998
Duration	38 months

Abstract

It has been possible to obtain perfect enzymes with new properties by the rational redesign of existing ones but the more usual experience is to obtain a less than perfect new catalyst. This project will develop combinatorial methods to guide the evolution of less than perfect new constructions towards perfection. For this to be possible it is necessary to select new catalysts from libraries of up to 1000000000 members. To do this effectively we shall link Cambridge Antibody Technology's skills in displaying enzyme proteins on the surface of fd phage and Bristol's expertise in screening large libraries of dehydrogenase enzymes for any new target substrate in E. coli. To understand perfect enzymes arising from unexpected sequences we shall determine crystal structures of mutant + an inactive coenzyme (tetrahydroNAD) + the target substrate.

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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