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Tubulin Vibration Modes Are in the Subterahertz Range, and Their Electromagnetic Absorption Is Affected by Water

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985882%3A_____%2F24%3A00597553" target="_blank" >RIV/67985882:_____/24:00597553 - isvavai.cz</a>

  • Result on the web

    <a href="https://pubs.acs.org/doi/10.1021/acs.jpclett.4c01553?goto=supporting-info&articleRef=test" target="_blank" >https://pubs.acs.org/doi/10.1021/acs.jpclett.4c01553?goto=supporting-info&articleRef=test</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1021/acs.jpclett.4c01553" target="_blank" >10.1021/acs.jpclett.4c01553</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Tubulin Vibration Modes Are in the Subterahertz Range, and Their Electromagnetic Absorption Is Affected by Water

  • Original language description

    Many proteins are thought to coordinate distant sites in their structures through a concerted action of global structural vibrations. However, the direct experimental spectroscopic detection of these vibration modes is rather elusive. We used normal-mode analysis to explore the dominant vibration modes of an all-atom model of the tubulin protein and described their characteristics using a large ensemble of tubulin structures. We quantified the frequency range of the normal vibrational modes to be in the subterahertz band, specifically between similar to 40 and similar to 160 GHz. Adding water layers to the model increases the frequencies of the low-frequency modes and narrows the frequency variations of the modes among the protein ensemble. We also showed how the electromagnetic absorption of tubulin vibration modes is affected by vibrational damping. These results contribute to our understanding of tubulin's vibrational and electromagnetic properties and provide a foundation for future attempts to control protein behavior via external electromagnetic fields.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10306 - Optics (including laser optics and quantum optics)

Result continuities

  • Project

    <a href="/en/project/GX20-06873X" target="_blank" >GX20-06873X: SubTHz on-chip devices for controlling protein nanomachines</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2024

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Journal of Physical Chemistry Letters

  • ISSN

    1948-7185

  • e-ISSN

  • Volume of the periodical

    15

  • Issue of the periodical within the volume

    32

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    9

  • Pages from-to

    8334-8342

  • UT code for WoS article

    001286300000001

  • EID of the result in the Scopus database

    2-s2.0-85200809239