Force Activation of a Multimeric Adhesive Protein through Domain Conformational Change

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dc.contributor.advisorKiang, Ching-Hwaen_US
dc.contributor.committeeMemberTao, Yizhi Janeen_US
dc.contributor.committeeMemberKono, Junichiroen_US
dc.creatorWijeratne, Sitaraen_US
dc.date.accessioned2013-07-24T19:50:30Zen_US
dc.date.accessioned2013-07-24T19:50:33Zen_US
dc.date.available2013-07-24T19:50:30Zen_US
dc.date.available2013-07-24T19:50:33Zen_US
dc.date.created2012-12en_US
dc.date.issued2013-07-24en_US
dc.date.submittedDecember 2012en_US
dc.date.updated2013-07-24T19:50:33Zen_US
dc.description.abstractThe force-induced activation of adhesive proteins such as von Willebrand Factor (VWF), which experience high hydrodynamic forces, is essential in initiating platelet adhesion. The importance of the mechanical force induced functional change is manifested in the multimeric VWF’s crucial role in blood coagulation, when high fluid shear stress activates pVWF multimers to bind platelets. Here we showed that a pathological level of high shear flow exposure of pVWF multimers results in domain conformational changes, and the subsequent shifts in the unfolding force allow us to use force as a marker to track the dynamic states of multimeric VWF. We found that shear-activated pVWF multimers (spVWF) are more resistant to mechanical unfolding than non-sheared pVWF multimers, as indicated in the higher peak unfolding force. These results provide insight into the mechanism of shear-induced activation of pVWF multimers.en_US
dc.format.mimetypeapplication/pdfen_US
dc.identifier.citationWijeratne, Sitara. "Force Activation of a Multimeric Adhesive Protein through Domain Conformational Change." (2013) Master’s Thesis, Rice University. <a href="https://hdl.handle.net/1911/71701">https://hdl.handle.net/1911/71701</a>.en_US
dc.identifier.slug123456789/ETD-2012-12-199en_US
dc.identifier.urihttps://hdl.handle.net/1911/71701en_US
dc.language.isoengen_US
dc.rightsCopyright is held by the author, unless otherwise indicated. Permission to reuse, publish, or reproduce the work beyond the bounds of fair use or other exemptions to copyright law must be obtained from the copyright holder.en_US
dc.subjectBiomoleculesen_US
dc.subjectProteinsen_US
dc.subjectSingle molecule manipulationen_US
dc.subjectAFM manipulation of a single moleculeen_US
dc.subjectVon Willebrand factoren_US
dc.titleForce Activation of a Multimeric Adhesive Protein through Domain Conformational Changeen_US
dc.typeThesisen_US
dc.type.materialTexten_US
thesis.degree.departmentApplied Physicsen_US
thesis.degree.disciplineNatural Sciencesen_US
thesis.degree.grantorRice Universityen_US
thesis.degree.levelMastersen_US
thesis.degree.nameMaster of Scienceen_US
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