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Nanosecond to millisecond dynamics in protein folding initiated by an ultrafast temperature jump
Reference
E08281
Principal Investigator / Supervisor
Professor David Smith
Co-Investigators /
Co-Supervisors
Professor Sheena Radford
Institution
University of Leeds
Department
Physics and Astronomy
Funding type
Research
Value (£)
108,811
Status
Completed
Type
Research Grant
Start date
03/11/1997
End date
03/11/1999
Duration
24 months
Abstract
We wish to extend the time domain accessible for spectroscopic studies of protein folding from milliseconds to the nanosecond regime. We have developed an ultrafast temperature jump apparatus and a mechanism for probing the subsequent folding using fluorescence. We wish to capitalise on this work by adding an experienced biophysicist to the project team and by replacing extremely unreliable second hand laser equipment. We shall test the system using apomyoglobin as a model protein and go on to study, with unprecedented time resolution, the refolding of the histidine containing protein HPr and modified human growth hormone which is of interest to our industrial partners, Duramed Europe Ltd. This project will also form the basis of a proposal for a time resolved CD or Raman spectroscopic probe of secondary structure formation in the near future.
Summary
unavailable
Committee
Closed Committee - Engineering & Biological Systems (EBS)
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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