SpringerProtocols: Abstract: 11. Analysis of PrP Conformation Using Circular Dichroism

11. Analysis of PrP Conformation Using Circular Dichroism

By: Sen Han³, Andrew F. Hill³

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The availability of recombinant prion proteins (recPrP) has been exploited as a model system to study PrP-mediated toxicity, conversion, and infectivity. According to the protein only hypothesis, the central event in the pathogenesis of prion diseases is the conversion of PrP^C to PrP^Sc. This involves a dramatic increase in β sheet conformation as PrP^C is converted to PrP^Sc, and it is widely believed that this conformational change affects the as-yet undefined function of PrP^C. Although there are many methods available to monitor for the changes in the structural makeup of PrP mutants and oligomers formed with respect to disease relevance, circular dichroism is one of the most popular methods used. In this chapter, we discuss the fundamental principles of circular dichroism and its current role and applications in prion disease research.

Affiliation(s): (3) Department of Biochemistry and Molecular Biology and Department of Pathology, Bio21 Molecular Science and Biotechnology Institute, Department of Pathology and Mental Health Research Institute of Victoria, University of Melbourne, Melbourne, Australia

Book Title: Prion Protein Protocols

Series: Methods in Molecular Biology | Volume: 459 | Pub. Date: Jun-04-2008 | Page Range: 145-159 | DOI: 10.1007/978-1-59745-234-2_11

Subject: Protein Science

Key Words: Circular dichroism - protein conformation - recombinant protein

References

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