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Theoretical Analysis of Dynamics of Kinesin Molecular Motors

[Image: see text] Kinesin is a typical molecular motor that can step processively on microtubules powered by hydrolysis of adenosine triphosphate (ATP) molecules, playing a critical role in intracellular transports. Its dynamical properties such as its velocity, stepping ratio, run length, dissociat...

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Autor principal: Xie, Ping
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2020
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7097908/
https://www.ncbi.nlm.nih.gov/pubmed/32226850
http://dx.doi.org/10.1021/acsomega.9b03738
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author Xie, Ping
author_facet Xie, Ping
author_sort Xie, Ping
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description [Image: see text] Kinesin is a typical molecular motor that can step processively on microtubules powered by hydrolysis of adenosine triphosphate (ATP) molecules, playing a critical role in intracellular transports. Its dynamical properties such as its velocity, stepping ratio, run length, dissociation rate, etc. as well as the load dependencies of these quantities have been well documented through single-molecule experimental methods. In particular, the run length shows a dramatic asymmetry with respect to the direction of the load, and the dissociation rate exhibits a slip–catch–slip bond behavior under the backward load. Here, an analytic theory was provided for the dynamics of kinesin motors under both forward and backward loads, explaining consistently and quantitatively the diverse available experimental results.
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spelling pubmed-70979082020-03-27 Theoretical Analysis of Dynamics of Kinesin Molecular Motors Xie, Ping ACS Omega [Image: see text] Kinesin is a typical molecular motor that can step processively on microtubules powered by hydrolysis of adenosine triphosphate (ATP) molecules, playing a critical role in intracellular transports. Its dynamical properties such as its velocity, stepping ratio, run length, dissociation rate, etc. as well as the load dependencies of these quantities have been well documented through single-molecule experimental methods. In particular, the run length shows a dramatic asymmetry with respect to the direction of the load, and the dissociation rate exhibits a slip–catch–slip bond behavior under the backward load. Here, an analytic theory was provided for the dynamics of kinesin motors under both forward and backward loads, explaining consistently and quantitatively the diverse available experimental results. American Chemical Society 2020-03-10 /pmc/articles/PMC7097908/ /pubmed/32226850 http://dx.doi.org/10.1021/acsomega.9b03738 Text en Copyright © 2020 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes.
spellingShingle Xie, Ping
Theoretical Analysis of Dynamics of Kinesin Molecular Motors
title Theoretical Analysis of Dynamics of Kinesin Molecular Motors
title_full Theoretical Analysis of Dynamics of Kinesin Molecular Motors
title_fullStr Theoretical Analysis of Dynamics of Kinesin Molecular Motors
title_full_unstemmed Theoretical Analysis of Dynamics of Kinesin Molecular Motors
title_short Theoretical Analysis of Dynamics of Kinesin Molecular Motors
title_sort theoretical analysis of dynamics of kinesin molecular motors
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7097908/
https://www.ncbi.nlm.nih.gov/pubmed/32226850
http://dx.doi.org/10.1021/acsomega.9b03738
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