https://w3id.org/np/RAA4sahbCvA0nXXU5T4kTFci4kTILoGBwEnxFtZAJEslQ/Head https://w3id.org/np/RAA4sahbCvA0nXXU5T4kTFci4kTILoGBwEnxFtZAJEslQ http://www.nanopub.org/nschema#hasAssertion https://w3id.org/np/RAA4sahbCvA0nXXU5T4kTFci4kTILoGBwEnxFtZAJEslQ/assertion https://w3id.org/np/RAA4sahbCvA0nXXU5T4kTFci4kTILoGBwEnxFtZAJEslQ http://www.nanopub.org/nschema#hasProvenance https://w3id.org/np/RAA4sahbCvA0nXXU5T4kTFci4kTILoGBwEnxFtZAJEslQ/provenance https://w3id.org/np/RAA4sahbCvA0nXXU5T4kTFci4kTILoGBwEnxFtZAJEslQ http://www.nanopub.org/nschema#hasPublicationInfo https://w3id.org/np/RAA4sahbCvA0nXXU5T4kTFci4kTILoGBwEnxFtZAJEslQ/pubinfo https://w3id.org/np/RAA4sahbCvA0nXXU5T4kTFci4kTILoGBwEnxFtZAJEslQ http://www.w3.org/1999/02/22-rdf-syntax-ns#type http://www.nanopub.org/nschema#Nanopublication https://w3id.org/np/RAA4sahbCvA0nXXU5T4kTFci4kTILoGBwEnxFtZAJEslQ/assertion https://w3id.org/delphi/resource/claim/buehler-2010-helix-sheet-02 http://purl.org/dc/terms/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. https://w3id.org/delphi/resource/claim/buehler-2010-helix-sheet-02 http://purl.org/dc/terms/type empirical-generalization https://w3id.org/delphi/resource/claim/buehler-2010-helix-sheet-02 http://www.w3.org/1999/02/22-rdf-syntax-ns#type https://w3id.org/delphi/ontology/Claim https://w3id.org/delphi/resource/claim/buehler-2010-helix-sheet-02 http://www.w3.org/2000/01/rdf-schema#label The alpha-to-beta transition is a universal deformation mechanism of alpha-helix-rich materials https://w3id.org/delphi/resource/claim/buehler-2010-helix-sheet-02 https://w3id.org/delphi/ontology/context 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 https://w3id.org/np/RAA4sahbCvA0nXXU5T4kTFci4kTILoGBwEnxFtZAJEslQ/provenance https://doi.org/10.1103/physrevlett.104.198304 http://purl.org/dc/terms/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 https://doi.org/10.1103/physrevlett.104.198304 http://purl.org/dc/terms/creator Zhao Qin, Markus J. 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Checked by build/check.py. https://w3id.org/np/RAA4sahbCvA0nXXU5T4kTFci4kTILoGBwEnxFtZAJEslQ/quote http://www.w3.org/ns/prov#hadPrimarySource https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=DOI:10.1103/physrevlett.104.198304&resultType=core&format=json https://w3id.org/np/RAA4sahbCvA0nXXU5T4kTFci4kTILoGBwEnxFtZAJEslQ/quote http://www.w3.org/ns/prov#wasQuotedFrom https://doi.org/10.1103/physrevlett.104.198304 https://w3id.org/np/RAA4sahbCvA0nXXU5T4kTFci4kTILoGBwEnxFtZAJEslQ/quote https://schema.org/text 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. https://w3id.org/np/RAA4sahbCvA0nXXU5T4kTFci4kTILoGBwEnxFtZAJEslQ/sourceChecksum http://spdx.org/rdf/terms#algorithm http://spdx.org/rdf/terms#checksumAlgorithm_sha256 https://w3id.org/np/RAA4sahbCvA0nXXU5T4kTFci4kTILoGBwEnxFtZAJEslQ/sourceChecksum http://spdx.org/rdf/terms#checksumValue ff3d9af312f17efad8cd63a0b625adaecca946740d011c905ff3e86d566bf132 https://w3id.org/np/RAA4sahbCvA0nXXU5T4kTFci4kTILoGBwEnxFtZAJEslQ/sourceChecksum http://www.w3.org/2000/01/rdf-schema#comment Checksum of the vendored text file inputs/2010-helix-sheet.abstract.txt, not of the publisher's copy. https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=DOI:10.1103/physrevlett.104.198304&resultType=core&format=json http://spdx.org/rdf/terms#checksum https://w3id.org/np/RAA4sahbCvA0nXXU5T4kTFci4kTILoGBwEnxFtZAJEslQ/sourceChecksum https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=DOI:10.1103/physrevlett.104.198304&resultType=core&format=json http://www.w3.org/1999/02/22-rdf-syntax-ns#type http://www.w3.org/ns/prov#Entity https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=DOI:10.1103/physrevlett.104.198304&resultType=core&format=json http://www.w3.org/2000/01/rdf-schema#label Abstract of Molecular Dynamics Simulation of theα-Helix toβ-Sheet Transition in Coiled Protein Filaments: Evidence for a Critical Filament Length Scale, as read https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=DOI:10.1103/physrevlett.104.198304&resultType=core&format=json https://schema.org/about https://doi.org/10.1103/physrevlett.104.198304 https://w3id.org/np/RAA4sahbCvA0nXXU5T4kTFci4kTILoGBwEnxFtZAJEslQ/pubinfo https://w3id.org/delphi/resource/domain/buehler-protein-materials http://www.w3.org/2000/01/rdf-schema#label buehler-protein-materials https://w3id.org/np/RAA4sahbCvA0nXXU5T4kTFci4kTILoGBwEnxFtZAJEslQ http://purl.org/dc/terms/created 2026-11-08T04:38:11.893Z https://w3id.org/np/RAA4sahbCvA0nXXU5T4kTFci4kTILoGBwEnxFtZAJEslQ http://purl.org/dc/terms/creator https://orcid.org/0009-0007-4948-9192 https://w3id.org/np/RAA4sahbCvA0nXXU5T4kTFci4kTILoGBwEnxFtZAJEslQ http://purl.org/dc/terms/license https://creativecommons.org/licenses/by/4.0/ https://w3id.org/np/RAA4sahbCvA0nXXU5T4kTFci4kTILoGBwEnxFtZAJEslQ http://purl.org/nanopub/x/hasNanopubType https://w3id.org/delphi/ontology/Claim https://w3id.org/np/RAA4sahbCvA0nXXU5T4kTFci4kTILoGBwEnxFtZAJEslQ http://purl.org/nanopub/x/introduces https://w3id.org/delphi/resource/claim/buehler-2010-helix-sheet-02 https://w3id.org/np/RAA4sahbCvA0nXXU5T4kTFci4kTILoGBwEnxFtZAJEslQ http://www.w3.org/2000/01/rdf-schema#label Zhao Qin et al. 2010 claim: The alpha-to-beta transition is a universal deformation mechanism of alpha-helix-rich materials https://w3id.org/np/RAA4sahbCvA0nXXU5T4kTFci4kTILoGBwEnxFtZAJEslQ https://w3id.org/delphi/ontology/domain https://w3id.org/delphi/resource/domain/buehler-protein-materials https://w3id.org/np/RAA4sahbCvA0nXXU5T4kTFci4kTILoGBwEnxFtZAJEslQ/sig http://purl.org/nanopub/x/hasAlgorithm RSA https://w3id.org/np/RAA4sahbCvA0nXXU5T4kTFci4kTILoGBwEnxFtZAJEslQ/sig http://purl.org/nanopub/x/hasPublicKey MIIBIjANBgkqhkiG9w0BAQEFAAOCAQ8AMIIBCgKCAQEAyFHtPB6p0mCjDozxlOY9CmO3nBm7Te3jFbXyLmM+G1tGe47Da0jYIbhkl9Oo1ZjxmCa3LCwlEqK8gj6hEIcL4ahW30JXh9HycfKVk1bugkzMEV15tJdTzAU3sGMFnbNsn43xY2LFLy45tApkRm5byEiM7oRRrooIdwoQKnP4Wzq/bfAoJ9qvW+MGkelyOTd1jbSt+KfmT7xKmDfWzAHddUlWwMX2QJOLxDaffOteTop6ZRgPiNmPJKA/S62Gac9XtSYT3oDkZ6/nr5cxxNLpOyxTf5FPISiCe11xYO/unYjY+mwnOfA8yhJIyx1l0O9I0vpOpn+E5TvyHJV+oSTrvwIDAQAB https://w3id.org/np/RAA4sahbCvA0nXXU5T4kTFci4kTILoGBwEnxFtZAJEslQ/sig http://purl.org/nanopub/x/hasSignature d6i3l2AvICNHi4oqgul8fYnt4lgeD7w+mepH1FTffiCKX6wjsnkZhykaym+Hnv/iMw2+c8KN95ZogYPxMSE5/7GzbmiXknF1oA0i+J3yGEFWuk3hTrS9m/sjUshH6RvNm6krG9JDBVR10nWWkHd3RaBms4ah3S5llsuSKK+TaIx/0doPsfhd8ufnMmsJSasxK6p2oxdeQjthiQVsv7RgqDJisTEKWq+PS/6cheti4O22roogpOV8eumJT9vN9fqgY/N/kFQVTbWor2MWP1zv0s/v5KyYuIkkRrJZ0UzyvFO9aWO0Kh+U5MCV8G+GlvE9RPPy0+oxmn9L3ii+NPkDWQ== https://w3id.org/np/RAA4sahbCvA0nXXU5T4kTFci4kTILoGBwEnxFtZAJEslQ/sig http://purl.org/nanopub/x/hasSignatureTarget https://w3id.org/np/RAA4sahbCvA0nXXU5T4kTFci4kTILoGBwEnxFtZAJEslQ https://w3id.org/np/RAA4sahbCvA0nXXU5T4kTFci4kTILoGBwEnxFtZAJEslQ/sig http://purl.org/nanopub/x/signedBy https://orcid.org/0009-0007-4948-9192