Phenomenological analysis of ATP dependence of motor proteins.

In this study, through phenomenological comparison of the velocity-force data of processive motor proteins, including conventional kinesin, cytoplasmic dynein and myosin V, I found that, the ratio between motor velocities of two different ATP concentrations is almost invariant for any substall, supe...

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Autor principal:	Yunxin Zhang
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/2f946053a4ed40f8a663e6b9993439ca
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spelling	oai:doaj.org-article:2f946053a4ed40f8a663e6b9993439ca2021-11-18T07:24:26ZPhenomenological analysis of ATP dependence of motor proteins.1932-620310.1371/journal.pone.0032717https://doaj.org/article/2f946053a4ed40f8a663e6b9993439ca2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22457719/?tool=EBIhttps://doaj.org/toc/1932-6203In this study, through phenomenological comparison of the velocity-force data of processive motor proteins, including conventional kinesin, cytoplasmic dynein and myosin V, I found that, the ratio between motor velocities of two different ATP concentrations is almost invariant for any substall, superstall or negative external loads. Therefore, the velocity of motors can be well approximated by a Michaelis-Menten like formula V = [ATP]k(F)L([ATP] + K(M)), with L the step size, and k(F) the external load F dependent rate of one mechanochemical cycle of motor motion in saturated ATP solution. The difference of Michaelis-Menten constant K(M) for substall, superstall and negative external load indicates, the configurations at which ATP molecule can bind to motor heads for these three cases might be different, though the expression of k(F) as a function of F might be unchanged for any external load F. Verifications of this Michaelis-Menten like formula has also been done by fitting to the recent experimental data.Yunxin ZhangPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 3, p e32717 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Yunxin Zhang Phenomenological analysis of ATP dependence of motor proteins.
description	In this study, through phenomenological comparison of the velocity-force data of processive motor proteins, including conventional kinesin, cytoplasmic dynein and myosin V, I found that, the ratio between motor velocities of two different ATP concentrations is almost invariant for any substall, superstall or negative external loads. Therefore, the velocity of motors can be well approximated by a Michaelis-Menten like formula V = [ATP]k(F)L([ATP] + K(M)), with L the step size, and k(F) the external load F dependent rate of one mechanochemical cycle of motor motion in saturated ATP solution. The difference of Michaelis-Menten constant K(M) for substall, superstall and negative external load indicates, the configurations at which ATP molecule can bind to motor heads for these three cases might be different, though the expression of k(F) as a function of F might be unchanged for any external load F. Verifications of this Michaelis-Menten like formula has also been done by fitting to the recent experimental data.
format	article
author	Yunxin Zhang
author_facet	Yunxin Zhang
author_sort	Yunxin Zhang
title	Phenomenological analysis of ATP dependence of motor proteins.
title_short	Phenomenological analysis of ATP dependence of motor proteins.
title_full	Phenomenological analysis of ATP dependence of motor proteins.
title_fullStr	Phenomenological analysis of ATP dependence of motor proteins.
title_full_unstemmed	Phenomenological analysis of ATP dependence of motor proteins.
title_sort	phenomenological analysis of atp dependence of motor proteins.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/2f946053a4ed40f8a663e6b9993439ca
work_keys_str_mv	AT yunxinzhang phenomenologicalanalysisofatpdependenceofmotorproteins
_version_	1718423465461022720

Phenomenological analysis of ATP dependence of motor proteins.

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