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Article

Glycosylation of prions and its effects on protein conformation relevant to amino acid mutations.

Journal of molecular graphics & modelling - 1 Apr 2000

Wong N K, Renouf D V, Lehmann S, Hounsell E F

Abstract excerpt

The three-dimensional coordinates from a nuclear magnetic resonance (NMR)-averaged structure containing residues 121-226 of mouse prion were used as the starting geometry for MD of prion either with or without glycan in both mutant and wild-type forms. The following mutants were studied: Asp-178 to Asn, Thr-183 to Ala, Phe-198 to Ser, Glu-200 to Lys, and Gln-217 to Arg. NMR data vs structural models were compared...

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Source

Identifiers

PMID: 10994516
DOI: 10.1016/S1093-3263(00)00044-9

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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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