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Article

Wild type and mutants of the HET-s(218-289) prion show different flexibility at fibrillar ends: a simulation study.

Proteins - 1 Mar 2014

Friedman Ran, Caflisch Amedeo

Abstract excerpt

The C-terminal segment (residues 218-289) of the HET-s protein of the filamentous fungus Podosporina anserina is a prion-forming domain. The structural model of the HET-s(218-289) amyloid fibril based on solid-state nuclear magnetic resonance (NMR) restraints shows a β solenoid topology which is comprised of a β-sheet core and interconnecting loops. For the single-point mutants Phe286Ala and Trp287Ala, slower...

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PMID: 24038616
DOI: 10.1002/prot.24402

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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