Chapter title |
Analysis of Prion Protein Conformation Using Circular Dichroism Spectroscopy
|
---|---|
Chapter number | 3 |
Book title |
Prions
|
Published in |
Methods in molecular biology, January 2017
|
DOI | 10.1007/978-1-4939-7244-9_3 |
Pubmed ID | |
Book ISBNs |
978-1-4939-7242-5, 978-1-4939-7244-9
|
Authors |
Laura J. Ellett, Vanessa A. Johanssen, Ellett, Laura J., Johanssen, Vanessa A. |
Abstract |
According to the protein-only hypothesis of prion propagation, the pathogenesis of prion disease is due to the misfolding of cellular PrP (PrP(C)) which gives rise to disease-associated PrP(Sc). This misfolding results in the predominantly α-helix secondary structure of PrP becoming increasingly β-sheet. Prion protein researchers often employ circular dichroism (CD) spectroscopy to rapidly analyze and identify the degree of α-helix and β-sheet content in their recombinant protein and peptide samples. CD is a nondestructive method of determining protein secondary structure and can be used to monitor the protein structural changes in various environments, e.g., pH and temperature. CD can also be used to investigate kinetic and thermodynamic characteristics of proteins and peptides. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
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Unknown | 8 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
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Student > Bachelor | 1 | 13% |
Professor | 1 | 13% |
Student > Ph. D. Student | 1 | 13% |
Researcher | 1 | 13% |
Other | 1 | 13% |
Other | 0 | 0% |
Unknown | 3 | 38% |
Readers by discipline | Count | As % |
---|---|---|
Environmental Science | 1 | 13% |
Biochemistry, Genetics and Molecular Biology | 1 | 13% |
Agricultural and Biological Sciences | 1 | 13% |
Immunology and Microbiology | 1 | 13% |
Chemistry | 1 | 13% |
Other | 0 | 0% |
Unknown | 3 | 38% |