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Chapter title |
Method for Folding of Recombinant Prion Protein to Soluble β-Sheet Secondary Structure
|
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Chapter number | 2 |
Book title |
Prions
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Published in |
Methods in molecular biology, January 2017
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DOI | 10.1007/978-1-4939-7244-9_2 |
Pubmed ID | |
Book ISBNs |
978-1-4939-7242-5, 978-1-4939-7244-9
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Authors |
Laura J. Ellett, Ellett, Laura J. |
Abstract |
A key event in the pathogenesis of prion diseases is the change in structure of the normal cellular form of the prion protein from a predominantly α-helix form to the β-sheet-rich prion protein found in disease-associated tissue. To allow more detailed structural research into PrP misfolding, it is necessary to have techniques which enable enrichment of the β-sheet content in recombinant PrP.This method describes the procedure for inducing β-folding of recombinant PrP to resemble a disease-associated structure and ultimately produce soluble β-folded recombinant PrP. |
Mendeley readers
The data shown below were compiled from readership statistics for 3 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 3 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Researcher | 2 | 67% |
Professor | 1 | 33% |
Readers by discipline | Count | As % |
---|---|---|
Biochemistry, Genetics and Molecular Biology | 1 | 33% |
Agricultural and Biological Sciences | 1 | 33% |
Immunology and Microbiology | 1 | 33% |