Award details

How unfolded is the unfolded state of proteins and can it direct folding pathways?

ReferenceB17948
Principal Investigator / Supervisor Professor Jon Waltho
Co-Investigators /
Co-Supervisors
Institution University of Sheffield
DepartmentMolecular Biology and Biotechnology
Funding typeResearch
Value (£) 197,604
StatusCompleted
TypeResearch Grant
Start date 15/02/2003
End date 14/01/2007
Duration47 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 TopicsX – not assigned to a current Research Topic
Research PriorityX – Research Priority information not available
Research Initiative X - not in an Initiative
Funding SchemeX – not Funded via a specific Funding Scheme
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