@prefix this: . @prefix sub: . @prefix np: . @prefix rdf: . @prefix prov: . @prefix npx: . @prefix dc: . @prefix xsd: . sub:Head { this: a np:Nanopublication; np:hasAssertion sub:assertion; np:hasProvenance sub:provenance; np:hasPublicationInfo sub:pubinfo . } sub:assertion { a ; dc:description "The alpha-helix to beta-sheet transition under deformation is a universal mechanism in alpha-helix-rich protein materials such as wool, hair, hoof and cellular proteins, and it explains why the transition is typically seen in filaments with long alpha-helical domains."; dc:type "empirical-generalization"; "The alpha-to-beta transition is a universal deformation mechanism of alpha-helix-rich materials"; "Zhao Qin et al., “Molecular Dynamics Simulation of theα-Helix toβ-Sheet Transition in Coiled Protein Filaments: Evidence for a Critical Filament Length Scale”, Physical Review Letters 104 (2010), doi:10.1103/physrevlett.104.198304; Abstract. Scope: Alpha-helix-rich protein materials" . } sub:provenance { a ; dc:bibliographicCitation "Zhao Qin, Markus J. Buehler. Molecular Dynamics Simulation of theα-Helix toβ-Sheet Transition in Coiled Protein Filaments: Evidence for a Critical Filament Length Scale. Physical Review Letters 104 (2010). doi:10.1103/physrevlett.104.198304"; dc:creator "Zhao Qin, Markus J. Buehler"; dc:date "2010"^^xsd:gYear; dc:identifier "doi:10.1103/physrevlett.104.198304", "pmid:20867006"; dc:title "Molecular Dynamics Simulation of theα-Helix toβ-Sheet Transition in Coiled Protein Filaments: Evidence for a Critical Filament Length Scale" . a prov:SoftwareAgent; "delphisci buehler-protein-materials claim extractor"; prov:actedOnBehalfOf ; . a ; "Claude Fable 5.1" . sub:assertion prov:wasAttributedTo ; prov:wasDerivedFrom , sub:quote; prov:wasGeneratedBy sub:extraction . sub:extraction a prov:Activity; prov:qualifiedAssociation sub:extractionPlan; prov:used , ; prov:wasAssociatedWith . sub:extractionPlan prov:hadPlan . sub:quote a prov:Entity; "Quoted from the published abstract as returned by Europe PMC (2010-helix-sheet.abstract.txt, sha256 ff3d9af312f17efad8cd63a0b625adaecca946740d011c905ff3e86d566bf132); the full text was not read (not in Europe PMC open-access subset). Checked by build/check.py."; prov:hadPrimarySource ; prov:wasQuotedFrom ; "The alpha-helix to beta-sheet transition (α-β transition) is a universal deformation mechanism in alpha-helix rich protein materials such as wool, hair, hoof, and cellular proteins." . sub:sourceChecksum ; "ff3d9af312f17efad8cd63a0b625adaecca946740d011c905ff3e86d566bf132"; "Checksum of the vendored text file inputs/2010-helix-sheet.abstract.txt, not of the publisher's copy." . a prov:Entity; sub:sourceChecksum; "Abstract of Molecular Dynamics Simulation of theα-Helix toβ-Sheet Transition in Coiled Protein Filaments: Evidence for a Critical Filament Length Scale, as read"; . } sub:pubinfo { "buehler-protein-materials" . this: dc:created "2026-11-08T04:38:11.893Z"^^xsd:dateTime; dc:creator ; dc:license ; npx:hasNanopubType ; npx:introduces ; "Zhao Qin et al. 2010 claim: The alpha-to-beta transition is a universal deformation mechanism of alpha-helix-rich materials"; . sub:sig npx:hasAlgorithm "RSA"; npx:hasPublicKey "MIIBIjANBgkqhkiG9w0BAQEFAAOCAQ8AMIIBCgKCAQEAyFHtPB6p0mCjDozxlOY9CmO3nBm7Te3jFbXyLmM+G1tGe47Da0jYIbhkl9Oo1ZjxmCa3LCwlEqK8gj6hEIcL4ahW30JXh9HycfKVk1bugkzMEV15tJdTzAU3sGMFnbNsn43xY2LFLy45tApkRm5byEiM7oRRrooIdwoQKnP4Wzq/bfAoJ9qvW+MGkelyOTd1jbSt+KfmT7xKmDfWzAHddUlWwMX2QJOLxDaffOteTop6ZRgPiNmPJKA/S62Gac9XtSYT3oDkZ6/nr5cxxNLpOyxTf5FPISiCe11xYO/unYjY+mwnOfA8yhJIyx1l0O9I0vpOpn+E5TvyHJV+oSTrvwIDAQAB"; npx:hasSignature "d6i3l2AvICNHi4oqgul8fYnt4lgeD7w+mepH1FTffiCKX6wjsnkZhykaym+Hnv/iMw2+c8KN95ZogYPxMSE5/7GzbmiXknF1oA0i+J3yGEFWuk3hTrS9m/sjUshH6RvNm6krG9JDBVR10nWWkHd3RaBms4ah3S5llsuSKK+TaIx/0doPsfhd8ufnMmsJSasxK6p2oxdeQjthiQVsv7RgqDJisTEKWq+PS/6cheti4O22roogpOV8eumJT9vN9fqgY/N/kFQVTbWor2MWP1zv0s/v5KyYuIkkRrJZ0UzyvFO9aWO0Kh+U5MCV8G+GlvE9RPPy0+oxmn9L3ii+NPkDWQ=="; npx:hasSignatureTarget this:; npx:signedBy . }