Myosin-V is an actin-associated processive molecular motor. Single
molecule experiments revealed that myosin-V walks in a stepwise fashion
with occasional backward steps. By combining the mechanical structure
of the motor with the ATP hydrolysis kinetics, we construct a dynamical
model that accounts for the stepwise processivity. The molecular
properties of the protein chains connecting the myosin heads are
important. A simple elastic model demonstrates that the stress transmitted
from the leading head to the trailing head leads to net forward motion.
The step-sizes are non-uniform. We also predict there are several
substeps. The translational speed and step-size distributions are
computed for several different conditions. The computed force-versus-velocity
curve shows that under an external load, myosin-V slows down. However,
the sizes of the steps remain the same.
%0 Journal Article
%1 Lan_2005_999
%A Lan, Ganhui
%A Sun, Sean X
%D 2005
%J Biophys. J.
%K Activation; Adenosine Chemical; Computer Conformation; Elasticity; Energy Enzyme Kinetics; Mechanical; Models, Molecular Molecular; Motor Movement; Myosin Protein Proteins; Relationship Simulation; Stability; Stress, Structure-Activity Transfer; Triphosphate; Type V;
%N 2
%P 999--1008
%R 10.1529/biophysj.104.047662
%T Dynamics of myosin-V processivity.
%U http://dx.doi.org/10.1529/biophysj.104.047662
%V 88
%X Myosin-V is an actin-associated processive molecular motor. Single
molecule experiments revealed that myosin-V walks in a stepwise fashion
with occasional backward steps. By combining the mechanical structure
of the motor with the ATP hydrolysis kinetics, we construct a dynamical
model that accounts for the stepwise processivity. The molecular
properties of the protein chains connecting the myosin heads are
important. A simple elastic model demonstrates that the stress transmitted
from the leading head to the trailing head leads to net forward motion.
The step-sizes are non-uniform. We also predict there are several
substeps. The translational speed and step-size distributions are
computed for several different conditions. The computed force-versus-velocity
curve shows that under an external load, myosin-V slows down. However,
the sizes of the steps remain the same.
@article{Lan_2005_999,
abstract = {Myosin-V is an actin-associated processive molecular motor. Single
molecule experiments revealed that myosin-V walks in a stepwise fashion
with occasional backward steps. By combining the mechanical structure
of the motor with the ATP hydrolysis kinetics, we construct a dynamical
model that accounts for the stepwise processivity. The molecular
properties of the protein chains connecting the myosin heads are
important. A simple elastic model demonstrates that the stress transmitted
from the leading head to the trailing head leads to net forward motion.
The step-sizes are non-uniform. We also predict there are several
substeps. The translational speed and step-size distributions are
computed for several different conditions. The computed force-versus-velocity
curve shows that under an external load, myosin-V slows down. However,
the sizes of the steps remain the same.},
added-at = {2009-06-03T11:20:58.000+0200},
author = {Lan, Ganhui and Sun, Sean X},
biburl = {https://www.bibsonomy.org/bibtex/2ffe1170f55abd2fb4be1b145a4408a33/hake},
description = {The whole bibliography file I use.},
doi = {10.1529/biophysj.104.047662},
institution = {Department of Mechanical Engineering, Johns Hopkins University, Baltimore,
Maryland, USA.},
interhash = {ec861de4fa10f30a99ee78a8d9fcccc6},
intrahash = {ffe1170f55abd2fb4be1b145a4408a33},
journal = {Biophys. J.},
keywords = {Activation; Adenosine Chemical; Computer Conformation; Elasticity; Energy Enzyme Kinetics; Mechanical; Models, Molecular Molecular; Motor Movement; Myosin Protein Proteins; Relationship Simulation; Stability; Stress, Structure-Activity Transfer; Triphosphate; Type V;},
month = Feb,
number = 2,
pages = {999--1008},
pii = {biophysj.104.047662},
pmid = {15556991},
timestamp = {2009-06-03T11:21:19.000+0200},
title = {Dynamics of myosin-V processivity.},
url = {http://dx.doi.org/10.1529/biophysj.104.047662},
volume = 88,
year = 2005
}