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Article

Structural instability of the prion protein upon M205S/R mutations revealed by molecular dynamics simulations.

Biophysical journal - 1 Jun 2006

Hirschberger Thomas, Stork Martina, Schropp Bernhard, Winklhofer Konstanze F, Tatzelt Jörg, Tavan Paul

Abstract excerpt

The point mutations M205S and M205R have been demonstrated to severely disturb the folding and maturation process of the cellular prion protein (PrP(C)). These disturbances have been interpreted as consequences of mutation-induced structural changes in PrP, which are suggested to involve helix 1 and its attachment to helix 3, because the mutated residue M205 of helix 3 is located at the interface of these two...

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Identifiers

PMID: 16513786
DOI: 10.1529/biophysj.105.075341
PMCID: PMC1459491

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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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