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Dissecting the mechanism of processive motility in single myosin V molecules

Record Type:	Electronic resources : Monograph/item
Title/Author:	Dissecting the mechanism of processive motility in single myosin V molecules
Author:	Purcell, Thomas J.
Description:	125 p.
Notes:	Adviser: James A. Spudich.
Notes:	Source: Dissertation Abstracts International, Volume: 65-04, Section: B, page: 1851.
Contained By:	Dissertation Abstracts International65-04B.
Subject:	Chemistry, Biochemistry.
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3128462
ISBN:	0496757245

Dissecting the mechanism of processive motility in single myosin V molecules
Purcell, Thomas J.

Dissecting the mechanism of processive motility in single myosin V molecules [electronic resource] - 125 p.

Adviser: James A. Spudich.

Thesis (Ph.D.)--Stanford University, 2004.

Efficient processive movement requires coordination of the two heads in myosin V. The myosin walks hand over hand. For a successful forward step to occur, the rear head must release before the lead head. The laser trap microscope was modified by addition of a feedback controlled piezoelectric stage, allowing a forward or reverse force to be applied on a single myosin V head during a transient binding event. These experiments reveal a force dependent state in the lead head of an asymmetrically walking myosin V. This state is kinetically stalled, allowing the rear head to complete its biochemical cycle and release from the actin.

ISBN: 0496757245Subjects--Topical Terms:

226900
Chemistry, Biochemistry.

Dissecting the mechanism of processive motility in single myosin V molecules
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520 # $a Efficient processive movement requires coordination of the two heads in myosin V. The myosin walks hand over hand. For a successful forward step to occur, the rear head must release before the lead head. The laser trap microscope was modified by addition of a feedback controlled piezoelectric stage, allowing a forward or reverse force to be applied on a single myosin V head during a transient binding event. These experiments reveal a force dependent state in the lead head of an asymmetrically walking myosin V. This state is kinetically stalled, allowing the rear head to complete its biochemical cycle and release from the actin.
520 # $a Myosin V is a processive actin based molecular motor. It is able to processively walk hand over hand on an actin filament in discrete 36 nm steps. The fundamental question about myosin V is how it is able to catalyze a large actin displacement using the energy of ATP. Myosin V consists of two heavy chain proteins joined by a coiled-coil dimerization domain. Each heavy chain has a globular N-terminal catalytic core domain containing the actin binding and ATPase activities. Immediately following the motor domain are six tandem light-chain binding motifs called IQ repeats. Each IQ repeat is complexed with a calmodulin or calmodulin-like essential light chain, forming a rigid extended region. Laser trap measurements show that this region functions as a lever arm. Mutants with different numbers of IQ repeats produce displacements proportional to the length of the lever arm. This relationship holds in two headed molecules that walk processively along the actin filament, as well as single headed mutants that produce a single step displacement per actin binding encounter.
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