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

Structural changes in a hydrophobic domain of the prion protein induced by hydration and by ala-->Val and pro-->Leu substitutions.

Journal of molecular biology - 28 Jul 2000

Inouye H, Bond J, Baldwin M A, Ball H L, Prusiner S B, Kirschner D A

Abstract excerpt

X-ray diffraction was used to study the structure of assemblies formed by synthetic peptide fragments of the prion protein (PrP) that include the hydrophobic domain implicated in the Gerstmann-Sträussler-Scheinker (GSS) mutation (P102L). The effects of hydration on polypeptide assembly and of Ala-->Val substitutions in the hydrophobic domain were characterized. Synthetic peptides included: (i) Syrian hamster...

Read the complete abstract on PubMed

Topics

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

Share to Gerstmann-Straussler-Scheinker Disease
Share to Hydrogen Bonding

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mesocricetus

Share to Peptide Fragments

Share to Prions

Share to Protein Folding

Share to X-Ray Diffraction

Source

Identifiers

PMID: 10903869
DOI: 10.1006/jmbi.2000.3926

Genes

GSS

Variants

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

Structural changes in a hydrophobic domain of the prion protein induced by hydration and by ala-->Val and pro-->Leu substitutions.PMID 10903869Read ↗

β-hairpin-mediated formation of structurally distinct multimers of neurotoxic prion peptides.Semantic proximity Read ↗

Prion and water: tight and dynamical hydration sites have a key role in structural stability.Semantic proximity Read ↗

The structural intolerance of the PrP alpha-fold for polar substitution of the helix-3 methionines.Semantic proximity Read ↗

The protonation state of histidine 111 regulates the aggregation of the evolutionary most conserved region of the human prion protein.Semantic proximity Read ↗

The Pathogenic A116V Mutation Enhances Ion-Selective Channel Formation by Prion Protein in Membranes.Semantic proximity Read ↗

Theoretical studies of sequence effects on the conformational properties of a fragment of the prion protein: implications for scrapie formation.Semantic proximity Read ↗

Hydration and packing are crucial to amyloidogenesis as revealed by pressure studies on transthyretin variants that either protect or worsen amyloid disease.Semantic proximity Read ↗

Helix H1 of the prion protein is rather stable against environmental perturbations: molecular dynamics of mutation and deletion variants of PrP(90-231).Semantic proximity Read ↗

Burial of the polymorphic residue 129 in amyloid fibrils of prion stop mutants.Semantic proximity Read ↗

Beta7E-beta132K salt bridge and sickle haemoglobin stability and conformation.Semantic proximity Read ↗

The key-role of tyrosine 155 in the mechanism of prion transconformation as highlighted by a study of sheep mutant peptides.Semantic proximity Read ↗

Probing subtle differences in the hydrogen exchange behavior of variants of the human alpha-lactalbumin molten globule using mass spectrometry.Semantic proximity Read ↗

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