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dc.contributor.authorQuigley, Andrew
dc.date.accessioned2016-11-18T17:37:25Z
dc.date.available2016-11-18T17:37:25Z
dc.identifier.urihttp://hdl.handle.net/10222/72283
dc.description.abstractThe collagen fibril is a fundamental unit in the mammalian class, providing strength and structure to various tissues. Here, I investigated the mechanical, morphological, and molecular properties of isolated collagen fibrils from two bovine forelimb tendons, which compose an energy storing - positional tendon pair. For each isolated fibril, two strips of glue were used to isolate a segment, which was pulled to rupture with an atomic force microscope. The stress-strain behavior of single fibrils was highly dependent on tendon type. Post-rupture AFM imaging showed that flexor fibrils were robust against plastic damage, while extensor fibrils were susceptible to plastic deformation. Second harmonic generation microscopy was used to investigate molecular organization pre- and post-rupture, and the molecular state was not altered by rupture in flexor fibrils, but was disrupted in extensor fibrils. The work shows that fibrils from distinct tendons follow unique mechanistic paths to failure.en_US
dc.language.isoenen_US
dc.subjectcollagen fibrilen_US
dc.subjectatomic force microscopeen_US
dc.titleCollagen fibrils from physiologically distinct tendons follow unique paths to failureen_US
dc.date.defence2016-11-01
dc.contributor.departmentDepartment of Physics & Atmospheric Scienceen_US
dc.contributor.degreeMaster of Scienceen_US
dc.contributor.external-examinern/aen_US
dc.contributor.graduate-coordinatorTheodore Moncheskyen_US
dc.contributor.thesis-readerManfred Jerichoen_US
dc.contributor.thesis-readerMike Leeen_US
dc.contributor.thesis-supervisorLaurent Kreplaken_US
dc.contributor.thesis-supervisorSamuel Veresen_US
dc.contributor.ethics-approvalNot Applicableen_US
dc.contributor.manuscriptsNot Applicableen_US
dc.contributor.copyright-releaseNot Applicableen_US
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