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https://w3id.org/np/RABHZUUeSyiShJvoX83cMoJ8zvoemiVqEPCbWOTxV7nUQ

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Content

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@prefix np: <http://www.nanopub.org/nschema#> .
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@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#> .

sub:Head {
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sub:assertion {
  <https://w3id.org/delphi/resource/claim/buehler-2007-hierarchies-04> a <https://w3id.org/delphi/ontology/Claim>;
    dc:description "In the hierarchical Bell model applied to alpha-helices, 3–4 parallel hydrogen bonds per turn are optimal for the protein's combined mechanical and thermodynamic stability, matching the 3.6 hydrogen bonds per turn of real alpha-helices.";
    dc:type "prediction";
    <http://www.w3.org/2000/01/rdf-schema#comment> "Notation basis: The optimum and the observed value are stated in the abstract; the objective being optimised is in the full text.";
    <http://www.w3.org/2000/01/rdf-schema#label> "Three to four parallel hydrogen bonds per turn is the mechanically and thermodynamically favoured number";
    <http://www.w3.org/2004/02/skos/core#notation> "b^{*} \\in \\{3, 4\\} \\quad (\\text{observed } b = 3.6 \\text{ H-bonds per turn})";
    <https://w3id.org/delphi/ontology/context> "Theodor Ackbarow et al., “Hierarchies, multiple energy barriers, and robustness govern the fracture mechanics of α-helical and β-sheet protein domains”, Proceedings of the National Academy of Sciences 104, 16410-16415 (2007), doi:10.1073/pnas.0705759104; Abstract. Scope: Alpha-helical protein domains" .
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sub:provenance {
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    dc:bibliographicCitation "Theodor Ackbarow, Xuefeng Chen, Sinan Keten, Markus J. Buehler. Hierarchies, multiple energy barriers, and robustness govern the fracture mechanics of α-helical and β-sheet protein domains. Proceedings of the National Academy of Sciences 104, 16410-16415 (2007). doi:10.1073/pnas.0705759104";
    dc:creator "Theodor Ackbarow, Xuefeng Chen, Sinan Keten, Markus J. Buehler";
    dc:date "2007"^^xsd:gYear;
    dc:identifier "PMC2034213", "doi:10.1073/pnas.0705759104", "pmid:17925444";
    dc:title "Hierarchies, multiple energy barriers, and robustness govern the fracture mechanics of α-helical and β-sheet protein domains" .
  
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    <https://schema.org/text> "We exemplify our model in a study of AHs, and show that 3-4 parallel HBs per turn are favorable in light of the protein's mechanical and thermodynamical stability, in agreement with experimental findings that AHs feature 3.6 HBs per turn." .
  
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