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How unfolded is the unfolded state of proteins and can it direct folding pathways?
Reference
B17948
Principal Investigator / Supervisor
Professor Jon Waltho
Co-Investigators /
Co-Supervisors
Institution
University of Sheffield
Department
Molecular Biology and Biotechnology
Funding type
Research
Value (£)
197,604
Status
Completed
Type
Research Grant
Start date
15/02/2003
End date
14/01/2007
Duration
47 months
Abstract
Recent NMR studies have led to the proposal that the unfolded state of proteins is not nearly as random as is commonly believed. If true, this will precipitate a re-evaluation of many experimental approaches that form the basis of our current understanding of protein folding. However, the interpretation of the original NMR data is not unique. We will carry out a series of experiments on the unfolded state of N- PGK to resolve the ambiguities of the original study. These experiments will further help resolve the key question of how larger and multidomain proteins manage to form so rapidly topologically- correct kinetic-intermediate states, and in doing so partition the residues destined for one domain from those destined for the other.
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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