https://w3id.org/np/RAZSD7NEG0D9wNPmhbomJEyF64B_NRw8R4sb_z9hJSXBE
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dc: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.";
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<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. Confirmation requires that load-bearing alpha-helix-rich biomaterials predominantly have helix segments longer than 26 residues and exhibit beta-sheet formation under large tensile strain.";
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