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
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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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
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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