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dc.contributor.authorPugno, Nicola M.
dc.contributor.authorGiesa, Tristan
dc.contributor.authorArslan, Melis
dc.contributor.authorBuehler, Markus J
dc.date.accessioned2017-05-17T14:47:37Z
dc.date.available2017-05-17T14:47:37Z
dc.date.issued2011-10
dc.date.submitted2011-09
dc.identifier.urihttp://hdl.handle.net/1721.1/109141
dc.description.abstractSilk is an exceptionally strong, extensible, and tough material made from simple protein building blocks. The molecular structure of dragline spider silk repeat units consists of semiamorphous and nanocrystalline β-sheet protein domains. Here we show by a series of computational experiments how the nanoscale properties of silk repeat units are scaled up to create macroscopic silk fibers with outstanding mechanical properties despite the presence of cavities, tears, and cracks. We demonstrate that the geometric confinement of silk fibrils to diameters of 50 ± 30 nm is critical to facilitate a powerful mechanism by which hundreds of thousands of protein domains synergistically resist deformation and failure to provide enhanced strength, extensibility, and toughness at the macroscale, closely matching experimentally measured mechanical properties. Through this mechanism silk fibers exploit the full potential of the nanoscale building blocks, regardless of the details of microscopic loading conditions and despite the presence of large defects. Experimental results confirm that silk fibers are composed of silk fibril bundles with diameters in the range of 20–150 nm, in agreement with our predicted length scale. Our study reveals a general mechanism to map nanoscale properties to the macroscale and provides a potent design strategy toward novel fiber and bulk nanomaterials through hierarchical structures.en_US
dc.description.sponsorshipUnited States. Army Research Office. Multidisciplinary University Research Initiative (Award 991NF-09-1-0541)en_US
dc.description.sponsorshipUnited States. Office of Naval Research (Presidential Early Career Awards for Scientists and Engineers Award N000141010562)en_US
dc.language.isoen_US
dc.publisherAmerican Chemical Societyen_US
dc.relation.isversionofhttp://dx.doi.org/10.1021/nl203108ten_US
dc.rightsArticle is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.en_US
dc.sourceOther Repositoryen_US
dc.titleFlaw-tolerance in silk fibrils explains strength, extensibility and toughness of spider silken_US
dc.title.alternativeNanoconfinement of Spider Silk Fibrils Begets Superior Strength, Extensibility, and Toughnessen_US
dc.typeArticleen_US
dc.identifier.citationGiesa,Tristan; Arslan, Melis; Pugno, Nicola M. and Buehler, Markus J. “Nanoconfinement of Spider Silk Fibrils Begets Superior Strength, Extensibility, and Toughness.” Nano Letters 11.11 (2011): 5038–5046. © 2011 American Chemical Societyen_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Civil and Environmental Engineeringen_US
dc.contributor.departmentMassachusetts Institute of Technology. Laboratory for Atomistic and Molecular Mechanicsen_US
dc.contributor.mitauthorGiesa, Tristan
dc.contributor.mitauthorArslan, Melis
dc.contributor.mitauthorBuehler, Markus J
dc.relation.journalNano Lettersen_US
dc.eprint.versionAuthor's final manuscripten_US
dc.type.urihttp://purl.org/eprint/type/JournalArticleen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dspace.orderedauthorsGiesa,Tristan; Arslan, Melis; Pugno, Nicola M.; Buehler, Markus J.en_US
dspace.embargo.termsNen_US
dc.identifier.orcidhttps://orcid.org/0000-0002-6601-9199
dc.identifier.orcidhttps://orcid.org/0000-0002-4173-9659
mit.licensePUBLISHER_POLICYen_US


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