2026-09-19T20:08:17Zhttps://dspace.mit.edu/server/oai/requestoai:dspace.mit.edu:1721.1/409152022-01-13T07:54:41Zcom_1721.1_7582com_1721.1_7581col_1721.1_131024
Matthew J. Lang.
Labno, Anna Kinga
Massachusetts Institute of Technology. Dept. of Physics.
Massachusetts Institute of Technology. Department of Physics
2008-03-27T18:22:55Z
2008-03-27T18:22:55Z
2007
2007
http://hdl.handle.net/1721.1/40915
212377213
Thesis (S.B.)--Massachusetts Institute of Technology, Dept. of Physics, 2007.
Includes bibliographical references (p. 42-53).
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.
by Anna Kinga Labno.
S.B.
53 p.
eng
Massachusetts Institute of Technology
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http://dspace.mit.edu/handle/1721.1/7582
Physics.
Experimental and theoretical investigation of mechanism of Kinesin motility
Thesis
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<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>
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