Počet záznamů: 1  

Electro-detachment of kinesin motor domain from microtubule in silico

  1. 1.
    SYSNO ASEP0570259
    Druh ASEPJ - Článek v odborném periodiku
    Zařazení RIVJ - Článek v odborném periodiku
    Poddruh JČlánek ve WOS
    NázevElectro-detachment of kinesin motor domain from microtubule in silico
    Tvůrce(i) Průša, Jiří (URE-Y)
    Cifra, Michal (URE-Y) RID, ORCID, SAI
    Celkový počet autorů2
    Zdroj.dok.Computational and Structural Biotechnology Journal. - : Elsevier - ISSN 2001-0370
    Roč. 21, FEB 2023 (2023), s. 1349-1361
    Poč.str.13 s.
    Forma vydáníTištěná - P
    Jazyk dok.eng - angličtina
    Země vyd.NL - Nizozemsko
    Klíč. slovaElectric field ; Proteins ; Tubulin ; Microtubules ; Molecular dynamics simulation
    Vědní obor RIVBH - Optika, masery a lasery
    Obor OECDBiophysics
    CEPGX20-06873X GA ČR - Grantová agentura ČR
    Způsob publikováníOmezený přístup
    Institucionální podporaURE-Y - RVO:67985882
    UT WOS000933953200001
    EID SCOPUS85147798567
    DOI10.1016/j.csbj.2023.01.018
    AnotaceKinesin is a motor protein essential in cellular functions, such as intracellular transport and cell-division, as well as for enabling nanoscopic transport in bio-nanotechnology. Therefore, for effective control of function for nanotechnological applications, it is important to be able to modify the function of kinesin. To cir-cumvent the limitations of chemical modifications, here we identify another potential approach for kinesin control: the use of electric forces. Using full-atom molecular dynamics simulations (247,358 atoms, total time 4.4 mu s), we demonstrate, for the first time, that the kinesin-1 motor domain can be detached from a microtubule by an intense electric field within the nanosecond timescale. We show that this effect is fielddirection dependent and field-strength dependent. A detailed analysis of the electric forces and the work carried out by electric field acting on the microtubule-kinesin system shows that it is the combined action of the electric field pulling on the-tubulin C-terminus and the electric-field-induced torque on the kinesin dipole moment that causes kinesin detachment from the microtubule. It is shown, for the first time in a mechanistic manner, that an electric field can dramatically affect molecular interactions in a heterologous functional protein assembly. Our results contribute to understanding of electromagnetic field-biomatter interactions on a molecular level, with potential biomedical and bio-nanotechnological applications for harnessing control of protein nanomotors.(c) 2023 The Author(s). Published by Elsevier B.V. on behalf of Research Network of Computational and Structural Biotechnology. This is an open access article under the CC BY-NC-ND license (http://creative-commons.org/licens es/by-nc-nd/4.0/)
    PracovištěÚstav fotoniky a elektroniky
    KontaktPetr Vacek, vacek@ufe.cz, Tel.: 266 773 413, 266 773 438, 266 773 488
    Rok sběru2024
    Elektronická adresa10.1016/j.csbj.2023.01.018
Počet záznamů: 1  

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