@prefix this: <https://w3id.org/np/RAgiuuVX246NEbUGKsKMWwh2zvX-i9mLedOzH2PlYwm6o> .
@prefix sub: <https://w3id.org/np/RAgiuuVX246NEbUGKsKMWwh2zvX-i9mLedOzH2PlYwm6o/> .
@prefix np: <http://www.nanopub.org/nschema#> .
@prefix rdf: <http://www.w3.org/1999/02/22-rdf-syntax-ns#> .
@prefix prov: <http://www.w3.org/ns/prov#> .
@prefix npx: <http://purl.org/nanopub/x/> .
@prefix dc: <http://purl.org/dc/terms/> .
@prefix xsd: <http://www.w3.org/2001/XMLSchema#> .

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    np:hasAssertion sub:assertion;
    np:hasProvenance sub:provenance;
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sub:assertion {
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    a <https://w3id.org/delphi/ontology/LLMClaimAssessment>;
    dc:description "Testing whether the empirical distribution of beta-strand lengths across proteomes peaks near the critical shear-strength length scale is a fast, high-powered bioinformatics analysis using the PDB and AlphaFold DB. While evolutionary causation is confounded by globular folding geometry, the stated claim is a correlation between strand-length prevalence and the shear-strength optimum, which is directly and decisively testable with open structural databases.";
    dc:subject <https://w3id.org/delphi/resource/concept/dataset-resolvability-0.2.0>;
    <http://www.w3.org/2000/01/rdf-schema#comment> "Proposed test with existing data: Run DSSP across non-redundant experimentally determined structures in the RCSB PDB (or AlphaFold DB proteomes) to compute the histogram of beta-strand lengths (in residues and H-bonds), and test whether the mode of the empirical distribution aligns with the predicted shear-strength optimum (around 3–4 H-bonds, i.e., 4–8 residues).";
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    <https://w3id.org/delphi/ontology/evidenceAgainst> "Observing a peak in beta-strand length around 4–7 residues confirms the correlation, but non-mechanical factors (globular domain diameter, folding kinetics, hydrophobic core packing) can produce the same length distribution even in proteins that never bear mechanical shear.";
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    prov:wasAttributedTo <https://w3id.org/delphi/resource/agent/delphisci-resolvability-assessor-gemini-4-argon-medium>;
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    a <https://w3id.org/delphi/ontology/LLMClaimAssessment>;
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    prov:wasAttributedTo <https://w3id.org/delphi/resource/agent/delphisci-resolvability-assessor-gemini-4-argon-medium>;
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  <https://w3id.org/delphi/resource/evidence/buehler-2008-hbond-confinement-04--gemini--dataset-1>
    a <https://w3id.org/delphi/ontology/EvidenceItem>;
    dc:description "Experimental protein structures across organisms from which beta-strand length distributions can be tabulated with DSSP";
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    prov:wasDerivedFrom <https://www.rcsb.org/> .
  
  <https://w3id.org/delphi/resource/model/gemini-4-argon-medium> a <https://w3id.org/delphi/ontology/LanguageModel>;
    dc:identifier "gemini-4-argon-medium";
    <http://www.w3.org/2000/01/rdf-schema#label> "Gemini 4 Argon" .
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  sub:assessmentPlan prov:hadPlan <https://github.com/fractastical/delphisci/blob/67fe5b156cfeca15a2ded33e0face4177d03101c/claim-sources/buehler-protein-materials/README.md> .
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sub:pubinfo {
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      "buehler-protein-materials" .
  
  this: dc:created "2026-11-08T04:48:50.317Z"^^xsd:dateTime;
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