BBSRC Portfolio Analyser
Award details
Main chain organisation in transient protein folding intermediates
Reference
B11477
Principal Investigator / Supervisor
Professor Anthony Clarke
Co-Investigators /
Co-Supervisors
Institution
University of Bristol
Department
Biochemistry
Funding type
Research
Value (£)
160,027
Status
Completed
Type
Research Grant
Start date
22/11/1999
End date
22/11/2002
Duration
36 months
Abstract
The degree to which the backbone conformation of a protein molecule is established in rapidly formed folding intermediates (I-states) is a subject of intense debate. Using a well- characterised immunoglobulin fold as a test-bed, the proposed experiments address this issue in two ways. Firstly, the backbone topology of intermediates will be examined by inserting disulphide cross-links at varying sequence spacings to map the change in conformational entropy in the intervening regions of the chain. Secondly, the extent to which I-states are discrete structures will be assessed by measuring the efficiency of propagation of stabilising and destabilising mutations to other regions of the molecule.
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
I accept the
terms and conditions of use
(opens in new window)
export PDF file
back to list
new search