https://w3id.org/np/RAZSD7NEG0D9wNPmhbomJEyF64B_NRw8R4sb_z9hJSXBE/Head https://w3id.org/np/RAZSD7NEG0D9wNPmhbomJEyF64B_NRw8R4sb_z9hJSXBE http://www.nanopub.org/nschema#hasAssertion https://w3id.org/np/RAZSD7NEG0D9wNPmhbomJEyF64B_NRw8R4sb_z9hJSXBE/assertion https://w3id.org/np/RAZSD7NEG0D9wNPmhbomJEyF64B_NRw8R4sb_z9hJSXBE http://www.nanopub.org/nschema#hasProvenance https://w3id.org/np/RAZSD7NEG0D9wNPmhbomJEyF64B_NRw8R4sb_z9hJSXBE/provenance https://w3id.org/np/RAZSD7NEG0D9wNPmhbomJEyF64B_NRw8R4sb_z9hJSXBE http://www.nanopub.org/nschema#hasPublicationInfo https://w3id.org/np/RAZSD7NEG0D9wNPmhbomJEyF64B_NRw8R4sb_z9hJSXBE/pubinfo https://w3id.org/np/RAZSD7NEG0D9wNPmhbomJEyF64B_NRw8R4sb_z9hJSXBE http://www.w3.org/1999/02/22-rdf-syntax-ns#type http://www.nanopub.org/nschema#Nanopublication https://w3id.org/np/RAZSD7NEG0D9wNPmhbomJEyF64B_NRw8R4sb_z9hJSXBE/assertion https://w3id.org/delphi/resource/agent/delphisci-resolvability-assessor-gemini-4-argon-medium http://www.w3.org/1999/02/22-rdf-syntax-ns#type http://www.w3.org/ns/prov#SoftwareAgent https://w3id.org/delphi/resource/agent/delphisci-resolvability-assessor-gemini-4-argon-medium http://www.w3.org/2000/01/rdf-schema#label delphisci dataset-resolvability assessor (Gemini 4 Argon) https://w3id.org/delphi/resource/agent/delphisci-resolvability-assessor-gemini-4-argon-medium http://www.w3.org/ns/prov#actedOnBehalfOf https://orcid.org/0009-0007-4948-9192 https://w3id.org/delphi/resource/agent/delphisci-resolvability-assessor-gemini-4-argon-medium https://w3id.org/delphi/ontology/usesModel https://w3id.org/delphi/resource/model/gemini-4-argon-medium https://w3id.org/delphi/resource/assessment/buehler-2010-helix-sheet-02--gemini http://purl.org/dc/terms/description The structural prediction implied by the claim—that fibrous proteins undergoing strain-induced alpha-to-beta transitions possess alpha-helical domains longer than the critical ~26-residue length scale—can be tested directly using sequence and structure annotations in UniProt and the PDB. Published WAXS, FTIR, and Raman studies on wool, hair, hard alpha-keratin, hagfish slime threads, and vimentin also confirm strain-induced beta-sheet formation in specific materials. However, because mechanical spectroscopy data are scattered across the literature and 'universal' is not quantitatively bounded, existing open data only partially resolve the claim. https://w3id.org/delphi/resource/assessment/buehler-2010-helix-sheet-02--gemini http://purl.org/dc/terms/subject https://w3id.org/delphi/resource/concept/dataset-resolvability-0.2.0 https://w3id.org/delphi/resource/assessment/buehler-2010-helix-sheet-02--gemini http://www.w3.org/1999/02/22-rdf-syntax-ns#type https://w3id.org/delphi/ontology/LLMClaimAssessment https://w3id.org/delphi/resource/assessment/buehler-2010-helix-sheet-02--gemini http://www.w3.org/2000/01/rdf-schema#comment Proposed test with existing data: Tabulate the length distribution of continuous alpha-helical coiled-coil domains in structural filament proteins (keratin, vimentin, lamin, myosin, fibrin) from UniProt and the PDB to test whether load-bearing filaments consistently exceed the 26-residue threshold, and cross-reference against published X-ray diffraction and Raman/FTIR tensile data documenting alpha-to-beta conversion. 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