Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Analysis of Prion Protein Structure Using Nuclear Magnetic Resonance Spectroscopy.

Methods in molecular biology (Clifton, N.J.) - 1 Jan 2017

Biljan Ivana, Ilc Gregor, Plavec Janez

Abstract excerpt

Nuclear magnetic resonance (NMR) spectroscopy is a powerful experimental tool for obtaining information on three-dimensional (3D) structures of proteins at atomic resolution. In inherited forms of prion diseases, misfolding of cellular prion protein, PrPC, into its pathological form, PrPSc, is caused by mutations in the human prion protein gene (PRNP). Understanding of the earliest stages of the conformational...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Carbon Isotopes
Share to Guanidine
Share to Inclusion Bodies

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Isotope Labeling

Share to Nitrogen Isotopes

Share to Prion Proteins

Share to Protein Conformation, alpha-Helical

Share to Protein Conformation, beta-Strand

Source

Identifiers

PMID: 28861781
DOI: 10.1007/978-1-4939-7244-9_4

Genes

PRNP

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Analysis of Prion Protein Structure Using Nuclear Magnetic Resonance Spectroscopy.PMID 28861781Read ↗

Understanding the Effect of Disease-Related Mutations on Human Prion Protein Structure: Insights From NMR Spectroscopy.Semantic proximity Read ↗

NMR structural studies of human cellular prion proteins.Semantic proximity Read ↗

Probing early misfolding events in prion protein mutants by NMR spectroscopy.Semantic proximity Read ↗

NMR structure of the human prion protein with the pathological Q212P mutation reveals unique structural features.Semantic proximity Read ↗

Backbone NMR assignments of the C-terminal domain of the human prion protein and its disease-associated T183A variant.Semantic proximity Read ↗

Toward the molecular basis of inherited prion diseases: NMR structure of the human prion protein with V210I mutation.Semantic proximity Read ↗

Structural rearrangements at physiological pH: nuclear magnetic resonance insights from the V210I human prion protein mutant.Semantic proximity Read ↗

Structural details of amyloid beta oligomers in complex with human prion protein as revealed by solid-state MAS NMR spectroscopySemantic proximity Read ↗

Intermolecular alignment in Y145Stop human prion protein amyloid fibrils probed by solid-state NMR spectroscopy.Semantic proximity Read ↗

A structural overview of the vertebrate prion proteins.Semantic proximity Read ↗

Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases.Semantic proximity Read ↗

The three-dimensional structure of prion protein: implications for prion disease.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.