Project: Research project

Project Details


Dr. Ropson proposes to investigate several members of the
intracellular lipid binding protein family (iLBPs) as a model for the study of
protein folding. As the model system, these proteins are characterized by
divergent sequences, but their native structures are nearly identical. They
also exhibit reversible two-state folding at equilibrium, but their folding
mechanisms and the energy landscapes appear to be different. The basic premise
is that, in their different folding pathways for these proteins, different
regions of the sequence and/or structure are responsible for initiating sites
or intermediate states for the folding of these divergent proteins. To test the
hypothesis, mass spectrometry and/or NMR will be used to measure
proton-deuterium exchange of amide protons. These measurements will enable the
PI to identify the different initiating sites/intermediate states. Structural
and mechanistic elucidations of the folding processes of these proteins will be
investigated by NMR and stopped-flow NMR and CD methods. Single-site mutant
proteins will be generated and studied for their effects on the transition
state in protein folding.
Effective start/end date9/30/008/31/06