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Design of proteins of prescribed structure: core-directed protein design

ReferenceB04756
Principal Investigator / Supervisor Professor Dek Woolfson
Co-Investigators /
Co-Supervisors
Dr Jonathan Cox
Institution University of Sussex
DepartmentBiology and Environmental Science
Funding typeResearch
Value (£) 143,746
StatusCompleted
TypeResearch Grant
Start date 01/10/1995
End date 01/10/1998
Duration36 months

Abstract

Attempts to design proteins de novo tend to produce molecules that contain secondary structure but lack fixed tertiary interactions. We describe a new approach to combat this failing. The method focuses on obtaining the set of hydrophobic amino acids that best specifies, or packs, the core of a given protein topology. The proposed procedure will involve: (1) Random mutagenesis at the hydrophobic core positions of the target protein. (2) Display of the resulting pool on the surface of phage. (3) Proteolytic selection to remove unfolded molecules from folded ones. (4) Affinity chromatography to separate intact protein-phage fusions from the other debris. (5) DNA sequencing to determine the primary structures of competently folded proteins.

Summary

unavailable
Committee Closed Committee - Biomolecular Sciences (BMS)
Research TopicsX – not assigned to a current Research Topic
Research PriorityX – Research Priority information not available
Research Initiative Biological Chemistry Initiative (BCI) [1995]
Funding SchemeX – not Funded via a specific Funding Scheme
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