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Organic Chemistry

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Wilson Protein

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Probing The Unfolding And The Stability Of The Last Four Metal Binding Domains Of Wilson Disease Protein Using Circular Dichroism And Novel Spectroscopic Techniques, Ibtesam Yaseen Alja’Afreh Dec 2014

Probing The Unfolding And The Stability Of The Last Four Metal Binding Domains Of Wilson Disease Protein Using Circular Dichroism And Novel Spectroscopic Techniques, Ibtesam Yaseen Alja’Afreh

Dissertations

Wilson disease protein is a copper-transporting P1B type ATPase. It has large N-terminal copper binding domain which is composed of six homologous sub-domains. Each of these six domains is ~72 residues and connected to one another by linking regions of various lengths. They all possess similar ferrodoxin fold, and metal-binding motif, MXCXXC.

The need of having six metal binding domains and the manner in which they are communicating with each other is not well understood. To better understand how the last four metal binding domains function, I pursued a detailed biophysical characterization of these domains. Using molecular biology I ...