Experimental and theoretical investigation of mechanism of Kinesin motility
Name
212377213-MIT.pdf
Description
Full printable version
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2.88 MB
Format
Adobe PDF
Checksum (MD5)
146bc72f3340217ce1083ffbed428d09
Author(s)
Labno, Anna Kinga
Advisor(s)
Matthew J. Lang.
Date Issued
2007
Publisher
Massachusetts Institute of Technology
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.
Description
Thesis (S.B.)--Massachusetts Institute of Technology, Dept. of Physics, 2007.
Includes bibliographical references (p. 42-53).
Subjects
Physics.
MIT Department
Massachusetts Institute of Technology. Department of Physics
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