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Probing Stability and Unfolding of the N-terminal Domains 5-6 of Wilson Protein

Faculty Mentor

Dr. Ramakrishna Guda

Department

Chemistry

Presentation Date

4-11-2014

Document Type

Poster

Abstract

The Wilson protein (ATP7B) is a copper transporting P1b type ATPase found in the liver, brain, and other organs. The N-terminal end consists of six copper binding domains which have a ferrodoxin βαββαβ fold with a CxxC motif. Despite similarities in copper binding affinities they interact differently with the HAH1 metallochaperone. Studying the stability of these domains will help understanding the differences in their functions. The stability of WLN5-6 was probed using several different methods: Dynamic light scattering (DLS), Circular dichroism (CD) and Fluorescence spectroscopy methods.

Previous studies show that WLN5-6 has a spherical shape and CD chemical unfolding studies indicate that mutants prepared had the same stability. Variations in Two Photon Absorption (2PA) cross-section are attributed to changes in local electric fields of the protein as confirmed from femtosecond fluorescence anisotropy and fluorescence lifetime. Present results show that the 2PA cross-sections can be used as a tool to probe local environments and unfolding of proteins.

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