{"id":{"repo_id":"mit","oai_identifier":"oai:dspace.mit.edu:1721.1/40915"},"canonical_url":"https://search.dev.ndltd.org/etd/mit/oai:dspace.mit.edu:1721.1/40915","repository":{"repo_id":"mit","name":"MIT","base_url":"https://dspace.mit.edu/oai/request"},"display":{"title":"Experimental and theoretical investigation of mechanism of Kinesin motility","abstract":"Kinesin is a motor protein capable of utilizing chemical energy from ATP hydrolysis to generate mechanical force to power its progressive motility along a microtubule track. The mechanism of motility has been a subject of extensive study for last decade. Recently, it has been proposed that novel element-cover strand-is essential in power-stroke-like force generation. In this work we attempt an experimental verification of this hypothesis by studying the mechanical properties, such as unloaded velocity, force velocity relationship, stall forces, processivity and step size of kinesin and mutants targeting cover strand region. We show that A9G and D11G mutants move slower and have lower stall force then the wild type molecule, but the mutants are ultraprocessive, make steps of 7nm and have a higher probability of taking backward steps suggesting that, indeed, force generating mechanism might been adversely affected by this mutation but it could also affect flexibility and directionality of the molecule.","abstract_html":"Kinesin is a motor protein capable of utilizing chemical energy from ATP hydrolysis to generate mechanical force to power its progressive motility along a microtubule track. The mechanism of motility has been a subject of extensive study for last decade. Recently, it has been proposed that novel element-cover strand-is essential in power-stroke-like force generation. In this work we attempt an experimental verification of this hypothesis by studying the mechanical properties, such as unloaded velocity, force velocity relationship, stall forces, processivity and step size of kinesin and mutants targeting cover strand region. We show that A9G and D11G mutants move slower and have lower stall force then the wild type molecule, but the mutants are ultraprocessive, make steps of 7nm and have a higher probability of taking backward steps suggesting that, indeed, force generating mechanism might been adversely affected by this mutation but it could also affect flexibility and directionality of the molecule.","abstract_has_math":false,"creators":["Labno, Anna Kinga"],"institution":"Massachusetts Institute of Technology","degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":"Massachusetts Institute of Technology. Dept. of Physics.","school":null,"contributors":[],"advisors":["Matthew J. Lang."],"committee_chairs":[],"committee_members":[],"year":2007,"date_issued":"2007","date_published":"2007","updated_at":"2026-07-22T22:21:24Z","subjects":["Physics."],"languages":["eng"],"rights":["M.I.T. theses are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission. See provided URL for inquiries about permission."],"rights_urls":["http://dspace.mit.edu/handle/1721.1/7582"],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/1721.1/40915","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Matthew J. Lang."]},{"key":"dc:contributor.department","label":"Department","values":["Massachusetts Institute of Technology. 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They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission. See provided URL for inquiries about permission."]},{"key":"dc:rights.uri","label":"Rights URI","values":["http://dspace.mit.edu/handle/1721.1/7582"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["http://hdl.handle.net/1721.1/40915"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Thesis (S.B.)--Massachusetts Institute of Technology, Dept. of Physics, 2007.","Includes bibliographical references (p. 42-53)."]},{"key":"dc:description.abstract","label":"Abstract","values":["Kinesin is a motor protein capable of utilizing chemical energy from ATP hydrolysis to generate mechanical force to power its progressive motility along a microtubule track. The mechanism of motility has been a subject of extensive study for last decade. Recently, it has been proposed that novel element-cover strand-is essential in power-stroke-like force generation. In this work we attempt an experimental verification of this hypothesis by studying the mechanical properties, such as unloaded velocity, force velocity relationship, stall forces, processivity and step size of kinesin and mutants targeting cover strand region. We show that A9G and D11G mutants move slower and have lower stall force then the wild type molecule, but the mutants are ultraprocessive, make steps of 7nm and have a higher probability of taking backward steps suggesting that, indeed, force generating mechanism might been adversely affected by this mutation but it could also affect flexibility and directionality of the molecule."]},{"key":"dc:description.degree","label":"Dc Description Degree","values":["S.B."]},{"key":"dc:title","label":"Title","values":["Experimental and theoretical investigation of mechanism of Kinesin motility"]}]}],"canonical_facts":{"dc:contributor.advisor":["Matthew J. Lang."],"dc:contributor.department":["Massachusetts Institute of Technology. Dept. of Physics."],"dc:contributor.other":["Massachusetts Institute of Technology. Dept. of Physics."],"dc:creator":["Labno, Anna Kinga"],"dc:date.accessioned":["2008-03-27T18:22:55Z"],"dc:date.available":["2008-03-27T18:22:55Z"],"dc:date.issued":["2007"],"dc:description":["Thesis (S.B.)--Massachusetts Institute of Technology, Dept. of Physics, 2007.","Includes bibliographical references (p. 42-53)."],"dc:description.abstract":["Kinesin is a motor protein capable of utilizing chemical energy from ATP hydrolysis to generate mechanical force to power its progressive motility along a microtubule track. The mechanism of motility has been a subject of extensive study for last decade. Recently, it has been proposed that novel element-cover strand-is essential in power-stroke-like force generation. In this work we attempt an experimental verification of this hypothesis by studying the mechanical properties, such as unloaded velocity, force velocity relationship, stall forces, processivity and step size of kinesin and mutants targeting cover strand region. We show that A9G and D11G mutants move slower and have lower stall force then the wild type molecule, but the mutants are ultraprocessive, make steps of 7nm and have a higher probability of taking backward steps suggesting that, indeed, force generating mechanism might been adversely affected by this mutation but it could also affect flexibility and directionality of the molecule."],"dc:description.degree":["S.B."],"dc:identifier.uri":["http://hdl.handle.net/1721.1/40915"],"dc:language.iso":["eng"],"dc:publisher":["Massachusetts Institute of Technology"],"dc:rights":["M.I.T. theses are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission. See provided URL for inquiries about permission."],"dc:rights.uri":["http://dspace.mit.edu/handle/1721.1/7582"],"dc:subject":["Physics."],"dc:title":["Experimental and theoretical investigation of mechanism of Kinesin motility"],"dc:type":["Thesis"]},"updated_at":"2026-07-22T22:21:24Z"}