{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/27741"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/27741","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Force studies of multiple kinesin-1 and EG5 molecular motors","abstract":"Kinesin-1 and Eg5 are molecular motors that are essential for eukaryotic cell growth and development. Kinesin-1 motors transport intracellular cargo along the microtubule cytoskeleton through and against the dense viscoelastic cytoplasm. Eg5 motors mediate proper mitotic, microtubule spindle assembly during cell division, and then stabilize these spindle structures through a balance between plus-end directed and minus-end directed forces along the filaments. Therefore, it is impmiant to understand how multiple kinesin-1 and Eg5 motors withstand competing forces, their structural rigidity under such loads, and how quickly they are able to rebind ifloosed from microtubules. Using a unique type of analysis for our optical trapping experiments, we are able to get motor binding stoichiometry inaccessible by previous techniques. With this information we characterize both motors comparing them to one another. We find that the release forces for both types of motors add linearly with the number of motors bound and that Eg5 has a weaker binding than that of kinesin -1. The stiffuess for the motor domains is comparable, yet we find that the average time to rebind for Eg5 decreases at higher concentrations while it does not for kinesin-1. This may indicate that there exists some weak interaction between kinesin-1 and microtubules keeping them close while unbound.","abstract_html":"Kinesin-1 and Eg5 are molecular motors that are essential for eukaryotic cell growth and development. Kinesin-1 motors transport intracellular cargo along the microtubule cytoskeleton through and against the dense viscoelastic cytoplasm. Eg5 motors mediate proper mitotic, microtubule spindle assembly during cell division, and then stabilize these spindle structures through a balance between plus-end directed and minus-end directed forces along the filaments. Therefore, it is impmiant to understand how multiple kinesin-1 and Eg5 motors withstand competing forces, their structural rigidity under such loads, and how quickly they are able to rebind ifloosed from microtubules. Using a unique type of analysis for our optical trapping experiments, we are able to get motor binding stoichiometry inaccessible by previous techniques. With this information we characterize both motors comparing them to one another. We find that the release forces for both types of motors add linearly with the number of motors bound and that Eg5 has a weaker binding than that of kinesin -1. The stiffuess for the motor domains is comparable, yet we find that the average time to rebind for Eg5 decreases at higher concentrations while it does not for kinesin-1. This may indicate that there exists some weak interaction between kinesin-1 and microtubules keeping them close while unbound.","abstract_has_math":false,"creators":["Graves, Evan Taclibon"],"institution":null,"degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Physics","degree_department":null,"school":null,"contributors":["Ha, Taekjip","Selvin, Paul R.","Oono, Yoshitsugu","Giannetta, Russell W."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2011,"date_issued":"2011-11-06T17:59:55Z","date_published":"2011-11-06T17:59:55Z","updated_at":"2026-07-22T22:25:27Z","subjects":["molecular motors"],"languages":["en"],"rights":["© Evan Taclibon Graves"],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/2142/27741","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Ha, Taekjip","Selvin, Paul R.","Oono, Yoshitsugu","Giannetta, Russell W."]},{"key":"dc:creator","label":"Author","values":["Graves, Evan Taclibon"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2011-11-06T17:59:55Z","10000-01-01","2009"]},{"key":"dc:type","label":"Dc Type","values":["Dissertation / Thesis","text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Physics"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["molecular motors"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["en"]},{"key":"dc:rights","label":"Dc Rights","values":["© Evan Taclibon Graves"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/27741"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Kinesin-1 and Eg5 are molecular motors that are essential for eukaryotic cell growth and development. Kinesin-1 motors transport intracellular cargo along the microtubule cytoskeleton through and against the dense viscoelastic cytoplasm. Eg5 motors mediate proper mitotic, microtubule spindle assembly during cell division, and then stabilize these spindle structures through a balance between plus-end directed and minus-end directed forces along the filaments. Therefore, it is impmiant to understand how multiple kinesin-1 and Eg5 motors withstand competing forces, their structural rigidity under such loads, and how quickly they are able to rebind ifloosed from microtubules. Using a unique type of analysis for our optical trapping experiments, we are able to get motor binding stoichiometry inaccessible by previous techniques. With this information we characterize both motors comparing them to one another. We find that the release forces for both types of motors add linearly with the number of motors bound and that Eg5 has a weaker binding than that of kinesin -1. The stiffuess for the motor domains is comparable, yet we find that the average time to rebind for Eg5 decreases at higher concentrations while it does not for kinesin-1. This may indicate that there exists some weak interaction between kinesin-1 and microtubules keeping them close while unbound.","Submitted by Megan O'Donnell (mnodonn2@illinois.edu) on 2011-11-06T17:59:55Z No. of bitstreams: 1 2009_Graves.pdf: 2697319 bytes, checksum: 51c49dfac5c8038038f0f1df75fa07e2 (MD5)","Made available in DSpace on 2011-11-06T17:59:55Z (GMT). No. of bitstreams: 1 2009_Graves.pdf: 2697319 bytes, checksum: 51c49dfac5c8038038f0f1df75fa07e2 (MD5) Previous issue date: 2009","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Megan O'Donnell (mnodonn2@illinois.edu) on 2011-11-06T17:59:55Z Item is restricted indefinitely.","Restriction data tranferred 2014-07-01T11:10:46-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: thesis/dissertation","thesis/dissertation","U of I Only"]},{"key":"dc:title","label":"Title","values":["Force studies of multiple kinesin-1 and EG5 molecular motors"]}]}],"canonical_facts":{"dc:contributor":["Ha, Taekjip","Selvin, Paul R.","Oono, Yoshitsugu","Giannetta, Russell W."],"dc:creator":["Graves, Evan Taclibon"],"dc:date":["2011-11-06T17:59:55Z","10000-01-01","2009"],"dc:description":["Kinesin-1 and Eg5 are molecular motors that are essential for eukaryotic cell growth and development. Kinesin-1 motors transport intracellular cargo along the microtubule cytoskeleton through and against the dense viscoelastic cytoplasm. Eg5 motors mediate proper mitotic, microtubule spindle assembly during cell division, and then stabilize these spindle structures through a balance between plus-end directed and minus-end directed forces along the filaments. Therefore, it is impmiant to understand how multiple kinesin-1 and Eg5 motors withstand competing forces, their structural rigidity under such loads, and how quickly they are able to rebind ifloosed from microtubules. Using a unique type of analysis for our optical trapping experiments, we are able to get motor binding stoichiometry inaccessible by previous techniques. With this information we characterize both motors comparing them to one another. We find that the release forces for both types of motors add linearly with the number of motors bound and that Eg5 has a weaker binding than that of kinesin -1. The stiffuess for the motor domains is comparable, yet we find that the average time to rebind for Eg5 decreases at higher concentrations while it does not for kinesin-1. This may indicate that there exists some weak interaction between kinesin-1 and microtubules keeping them close while unbound.","Submitted by Megan O'Donnell (mnodonn2@illinois.edu) on 2011-11-06T17:59:55Z No. of bitstreams: 1 2009_Graves.pdf: 2697319 bytes, checksum: 51c49dfac5c8038038f0f1df75fa07e2 (MD5)","Made available in DSpace on 2011-11-06T17:59:55Z (GMT). No. of bitstreams: 1 2009_Graves.pdf: 2697319 bytes, checksum: 51c49dfac5c8038038f0f1df75fa07e2 (MD5) Previous issue date: 2009","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Megan O'Donnell (mnodonn2@illinois.edu) on 2011-11-06T17:59:55Z Item is restricted indefinitely.","Restriction data tranferred 2014-07-01T11:10:46-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: thesis/dissertation","thesis/dissertation","U of I Only"],"dc:identifier":["http://hdl.handle.net/2142/27741"],"dc:language":["en"],"dc:rights":["© Evan Taclibon Graves"],"dc:subject":["molecular motors"],"dc:title":["Force studies of multiple kinesin-1 and EG5 molecular motors"],"dc:type":["Dissertation / Thesis","text"],"thesis:degree_discipline":["Physics"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."]},"updated_at":"2026-07-22T22:25:27Z"}