Nonthermal excitation effects mediated by sub-terahertz radiation on hydrogen exchange in ubiquitin
Copyright © 2021 Biophysical Society. Published by Elsevier Inc. All rights reserved..
Water dynamics in the hydration layers of biomolecules play crucial roles in a wide range of biological functions. A hydrated protein contains multiple components of diffusional and vibrational dynamics of water and protein, which may be coupled at ∼0.1-THz frequency (10-ps timescale) at room temperature. However, the microscopic description of biomolecular functions based on various modes of protein-water-coupled motions remains elusive. A novel approach for perturbing the hydration dynamics in the subterahertz frequency range and probing them at the atomic level is therefore warranted. In this study, we investigated the effect of klystron-based, intense 0.1-THz excitation on the slow dynamics of ubiquitin using NMR-based measurements of hydrogen-deuterium exchange. We demonstrated that the subterahertz irradiation accelerated the hydrogen-deuterium exchange of the amides located in the interior of the protein and hydrophobic surfaces while decelerating this exchange in the amides located in the surface loop and short 310 helix regions. This subterahertz-radiation-induced effect was qualitatively contradictory to the increased-temperature-induced effect. Our results suggest that the heterogeneous water dynamics occurring at the protein-water interface include components that are nonthermally excited by the subterahertz radiation. Such subterahertz-excited components may be linked to the slow function-related dynamics of the protein.
Medienart: |
E-Artikel |
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Erscheinungsjahr: |
2021 |
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Erschienen: |
2021 |
Enthalten in: |
Zur Gesamtaufnahme - volume:120 |
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Enthalten in: |
Biophysical journal - 120(2021), 12 vom: 15. Juni, Seite 2386-2393 |
Sprache: |
Englisch |
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Beteiligte Personen: |
Tokunaga, Yuji [VerfasserIn] |
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Links: |
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Themen: |
059QF0KO0R |
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Anmerkungen: |
Date Completed 02.07.2021 Date Revised 16.07.2022 published: Print-Electronic Citation Status MEDLINE |
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doi: |
10.1016/j.bpj.2021.04.013 |
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funding: |
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Förderinstitution / Projekttitel: |
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PPN (Katalog-ID): |
NLM324477848 |
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520 | |a Copyright © 2021 Biophysical Society. Published by Elsevier Inc. All rights reserved. | ||
520 | |a Water dynamics in the hydration layers of biomolecules play crucial roles in a wide range of biological functions. A hydrated protein contains multiple components of diffusional and vibrational dynamics of water and protein, which may be coupled at ∼0.1-THz frequency (10-ps timescale) at room temperature. However, the microscopic description of biomolecular functions based on various modes of protein-water-coupled motions remains elusive. A novel approach for perturbing the hydration dynamics in the subterahertz frequency range and probing them at the atomic level is therefore warranted. In this study, we investigated the effect of klystron-based, intense 0.1-THz excitation on the slow dynamics of ubiquitin using NMR-based measurements of hydrogen-deuterium exchange. We demonstrated that the subterahertz irradiation accelerated the hydrogen-deuterium exchange of the amides located in the interior of the protein and hydrophobic surfaces while decelerating this exchange in the amides located in the surface loop and short 310 helix regions. This subterahertz-radiation-induced effect was qualitatively contradictory to the increased-temperature-induced effect. Our results suggest that the heterogeneous water dynamics occurring at the protein-water interface include components that are nonthermally excited by the subterahertz radiation. Such subterahertz-excited components may be linked to the slow function-related dynamics of the protein | ||
650 | 4 | |a Journal Article | |
650 | 4 | |a Research Support, Non-U.S. Gov't | |
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650 | 7 | |a Hydrogen |2 NLM | |
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700 | 1 | |a Tanaka, Masahito |e verfasserin |4 aut | |
700 | 1 | |a Iida, Hitoshi |e verfasserin |4 aut | |
700 | 1 | |a Kinoshita, Moto |e verfasserin |4 aut | |
700 | 1 | |a Tojima, Yuya |e verfasserin |4 aut | |
700 | 1 | |a Takeuchi, Koh |e verfasserin |4 aut | |
700 | 1 | |a Imashimizu, Masahiko |e verfasserin |4 aut | |
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