Contribution of specific residues of the β-solenoid fold to HET-s prion function, amyloid structure and stability.

Contribution of specific residues of the β-solenoid fold to HET-s prion function, amyloid structure and stability.

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 ado...

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Main Authors: Asen Daskalov, Matthias Gantner, Marielle Aulikki Wälti, Thierry Schmidlin, Celestine N Chi, Christian Wasmer, Anne Schütz, Johanna Ceschin, Corinne Clavé, Sandra Cescau, Beat Meier, Roland Riek, Sven J Saupe
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2014-06-01
Series:PLoS Pathogens
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24945274/pdf/?tool=EBI

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