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Article

Structural and dynamic properties of the human prion protein.

Biophysical journal - 4 Mar 2014

Chen Wei, van der Kamp Marc W, Daggett Valerie

Abstract excerpt

Prion diseases involve the conformational conversion of the cellular prion protein (PrP(C)) to its misfolded pathogenic form (PrP(Sc)). To better understand the structural mechanism of this conversion, we performed extensive all-atom, explicit-solvent molecular-dynamics simulations for three structures of the wild-type human PrP (huPrP) at different pH values and temperatures. Residue 129 is polymorphic, being...

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Identifiers

PMID: 24606939
DOI: 10.1016/j.bpj.2013.12.053
PMCID: PMC4026773

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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