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National Science Foundation
Experimental Program to
Stimulate Competitive Research

Summer Undergraduate Diversity Research Program

April Woods
Faculty Advisor
Dr. Michele McGuirl
Division of Biological Sciences

Designing a Clone for a High Affinity Copper(II)
Binding Site of the Prion Protein

Abstract

Prion diseases are infectious diseases of the brain, responsible for a variety of neurodegenerative diseases. The prion protein (PrP) contains several Copper binding sites ranging from low binding affinity to high binding affinity. In order to study the role of the CuII binding sites in the process of conversion to the protein's infectious state, we have isolated a portion of the prion gene containing one high affinity CuII binding site. This gene segment was cloned into the pProEx-Hta vector. This vector contains a series of six histidines, which will become incorporated into the recombinant protein. The His tag will bind to a protein column and facilitate purification of the protein. The His tag will be removed by protease digestion and further study of the copper binding site will be done.

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