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Article

Atomic insights into the effects of pathological mutants through the disruption of hydrophobic core in the prion protein.

Scientific reports - 16 Dec 2019

Lee Juhwan, Chang Iksoo, Yu Wookyung

Abstract excerpt

Destabilization of prion protein induces a conformational change from normal prion protein (PrPC) to abnormal prion protein (PrPSC). Hydrophobic interaction is the main driving force for protein folding, and critically affects the stability and solvability. To examine the importance of the hydrophobic core in the PrP, we chose six amino acids (V176, V180, T183, V210, I215, and Y218) that make up the hydrophobic...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 31844149
DOI: 10.1038/s41598-019-55661-2
PMCID: PMC6915724

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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