Contribution of Specific Residues of the [beta]-Solenoid Fold to HET-s Prion Function, Amyloid Struc...
Contribution of Specific Residues of the [beta]-Solenoid Fold to HET-s Prion Function, Amyloid Structure and Stability: e1004158
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San Francisco: Public Library of Science
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English
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San Francisco: Public Library of Science
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The [Het-s] prion of the fungus Podospora anserina represents a good model system for studying the structure-function relationship in amyloid proteins because a high resolution solid-state NMR structure of the amyloid prion form of the HET-s prion forming domain (PFD) is available. The HET-s PFD adopts a specific β-solenoid fold with two rungs of β...
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Contribution of Specific Residues of the [beta]-Solenoid Fold to HET-s Prion Function, Amyloid Structure and Stability: e1004158
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TN_cdi_proquest_journals_1547573107
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_1547573107
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ISSN
1553-7366
E-ISSN
1553-7374
DOI
10.1371/journal.ppat.1004158
