https://w3id.org/np/RAKz03xd315wTSStuEyUNRuxcrFoulqqnBTO82hfZptsQ/Head https://w3id.org/np/RAKz03xd315wTSStuEyUNRuxcrFoulqqnBTO82hfZptsQ http://www.nanopub.org/nschema#hasAssertion https://w3id.org/np/RAKz03xd315wTSStuEyUNRuxcrFoulqqnBTO82hfZptsQ/assertion https://w3id.org/np/RAKz03xd315wTSStuEyUNRuxcrFoulqqnBTO82hfZptsQ http://www.nanopub.org/nschema#hasProvenance https://w3id.org/np/RAKz03xd315wTSStuEyUNRuxcrFoulqqnBTO82hfZptsQ/provenance https://w3id.org/np/RAKz03xd315wTSStuEyUNRuxcrFoulqqnBTO82hfZptsQ http://www.nanopub.org/nschema#hasPublicationInfo https://w3id.org/np/RAKz03xd315wTSStuEyUNRuxcrFoulqqnBTO82hfZptsQ/pubinfo https://w3id.org/np/RAKz03xd315wTSStuEyUNRuxcrFoulqqnBTO82hfZptsQ http://www.w3.org/1999/02/22-rdf-syntax-ns#type http://www.nanopub.org/nschema#Nanopublication https://w3id.org/np/RAKz03xd315wTSStuEyUNRuxcrFoulqqnBTO82hfZptsQ/assertion https://w3id.org/delphi/resource/claim/buehler-2007-tropocollagen-entropic-01 http://purl.org/dc/terms/description A single tropocollagen molecule under tension is dominated by entropic elasticity at small deformation and crosses over to energetic elasticity at larger deformation, where hydrogen bonds stretch and break and then covalent backbone bonds deform, ending in molecular fracture. https://w3id.org/delphi/resource/claim/buehler-2007-tropocollagen-entropic-01 http://purl.org/dc/terms/type simulation-result https://w3id.org/delphi/resource/claim/buehler-2007-tropocollagen-entropic-01 http://www.w3.org/1999/02/22-rdf-syntax-ns#type https://w3id.org/delphi/ontology/Claim https://w3id.org/delphi/resource/claim/buehler-2007-tropocollagen-entropic-01 http://www.w3.org/2000/01/rdf-schema#label Tropocollagen stretches entropically at small deformation and energetically at large https://w3id.org/delphi/resource/claim/buehler-2007-tropocollagen-entropic-01 https://w3id.org/delphi/ontology/context Markus J. Buehler et al., “Entropic Elasticity Controls Nanomechanics of Single Tropocollagen Molecules”, Biophysical Journal 93, 37-43 (2007), doi:10.1529/biophysj.106.102616; Abstract. Scope: Single tropocollagen molecules in molecular simulation https://w3id.org/np/RAKz03xd315wTSStuEyUNRuxcrFoulqqnBTO82hfZptsQ/provenance https://doi.org/10.1529/biophysj.106.102616 http://purl.org/dc/terms/bibliographicCitation Markus J. Buehler, Sophie Y. Wong. Entropic Elasticity Controls Nanomechanics of Single Tropocollagen Molecules. Biophysical Journal 93, 37-43 (2007). doi:10.1529/biophysj.106.102616 https://doi.org/10.1529/biophysj.106.102616 http://purl.org/dc/terms/creator Markus J. Buehler, Sophie Y. 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Checked by build/check.py. https://w3id.org/np/RAKz03xd315wTSStuEyUNRuxcrFoulqqnBTO82hfZptsQ/quote http://www.w3.org/ns/prov#hadPrimarySource https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=DOI:10.1529/biophysj.106.102616&resultType=core&format=json https://w3id.org/np/RAKz03xd315wTSStuEyUNRuxcrFoulqqnBTO82hfZptsQ/quote http://www.w3.org/ns/prov#wasQuotedFrom https://doi.org/10.1529/biophysj.106.102616 https://w3id.org/np/RAKz03xd315wTSStuEyUNRuxcrFoulqqnBTO82hfZptsQ/quote https://schema.org/text For small deformation, we observe a dominance of entropic elasticity. At larger deformation, we find a transition to energetic elasticity, which is characterized by first stretching and breaking of hydrogen bonds, followed by deformation of covalent bonds in the protein backbone, eventually leading to molecular fracture. https://w3id.org/np/RAKz03xd315wTSStuEyUNRuxcrFoulqqnBTO82hfZptsQ/sourceChecksum http://spdx.org/rdf/terms#algorithm http://spdx.org/rdf/terms#checksumAlgorithm_sha256 https://w3id.org/np/RAKz03xd315wTSStuEyUNRuxcrFoulqqnBTO82hfZptsQ/sourceChecksum http://spdx.org/rdf/terms#checksumValue 3aa9bd61023729ed67ddfd52bcc743b0f2a9aabbcdbeb8461e8c73a87c898410 https://w3id.org/np/RAKz03xd315wTSStuEyUNRuxcrFoulqqnBTO82hfZptsQ/sourceChecksum http://www.w3.org/2000/01/rdf-schema#comment Checksum of the vendored text file inputs/2007-tropocollagen-entropic.abstract.txt, not of the publisher's copy. https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=DOI:10.1529/biophysj.106.102616&resultType=core&format=json http://spdx.org/rdf/terms#checksum https://w3id.org/np/RAKz03xd315wTSStuEyUNRuxcrFoulqqnBTO82hfZptsQ/sourceChecksum https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=DOI:10.1529/biophysj.106.102616&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:10.1529/biophysj.106.102616&resultType=core&format=json http://www.w3.org/2000/01/rdf-schema#label Abstract of Entropic Elasticity Controls Nanomechanics of Single Tropocollagen Molecules, as read https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=DOI:10.1529/biophysj.106.102616&resultType=core&format=json https://schema.org/about https://doi.org/10.1529/biophysj.106.102616 https://w3id.org/np/RAKz03xd315wTSStuEyUNRuxcrFoulqqnBTO82hfZptsQ/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/RAKz03xd315wTSStuEyUNRuxcrFoulqqnBTO82hfZptsQ http://purl.org/dc/terms/created 2026-11-08T04:38:11.893Z https://w3id.org/np/RAKz03xd315wTSStuEyUNRuxcrFoulqqnBTO82hfZptsQ http://purl.org/dc/terms/creator https://orcid.org/0009-0007-4948-9192 https://w3id.org/np/RAKz03xd315wTSStuEyUNRuxcrFoulqqnBTO82hfZptsQ http://purl.org/dc/terms/license https://creativecommons.org/licenses/by/4.0/ https://w3id.org/np/RAKz03xd315wTSStuEyUNRuxcrFoulqqnBTO82hfZptsQ http://purl.org/nanopub/x/hasNanopubType https://w3id.org/delphi/ontology/Claim https://w3id.org/np/RAKz03xd315wTSStuEyUNRuxcrFoulqqnBTO82hfZptsQ http://purl.org/nanopub/x/introduces https://w3id.org/delphi/resource/claim/buehler-2007-tropocollagen-entropic-01 https://w3id.org/np/RAKz03xd315wTSStuEyUNRuxcrFoulqqnBTO82hfZptsQ http://www.w3.org/2000/01/rdf-schema#label Markus J. 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