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Protein orientation in time-dependent electric fields: orientation before destruction
Uppsala University, Disciplinary Domain of Science and Technology, Physics, Department of Physics and Astronomy, Materials Theory.
Uppsala University, Disciplinary Domain of Science and Technology, Physics, Department of Physics and Astronomy, Chemical and Bio-Molecular Physics. ty of Applied Sciences Technikum Wien, Wien, Austria.
Uppsala University, Disciplinary Domain of Science and Technology, Physics, Department of Physics and Astronomy.ORCID iD: 0000-0002-8130-6823
Uppsala University, Disciplinary Domain of Science and Technology, Physics, Department of Physics and Astronomy, Materials Theory.ORCID iD: 0000-0002-1482-2182
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2021 (English)In: Biophysical Journal, ISSN 0006-3495, E-ISSN 1542-0086, Vol. 120, no 17, p. 3709-3717, article id S0006-3495(21)00603-2Article in journal (Refereed) Published
Abstract [en]

Proteins often have nonzero electric dipole moments, making them interact with external electric fields and offering a means for controlling their orientation. One application that is known to benefit from orientation control is single-particle imaging with x-ray free-electron lasers, in which diffraction is recorded from proteins in the gas phase to determine their structures. To this point, theoretical investigations into this phenomenon have assumed that the field experienced by the proteins is constant or a perfect step function, whereas any real-world pulse will be smooth. Here, we explore the possibility of orienting gas-phase proteins using time-dependent electric fields. We performed ab initio simulations to estimate the field strength required to break protein bonds, with 45 V/nm as a breaking point value. We then simulated ubiquitin in time-dependent electric fields using classical molecular dynamics. The minimal field strength required for orientation within 10 ns was on the order of 0.5 V/nm. Although high fields can be destructive for the structure, the structures in our simulations were preserved until orientation was achieved regardless of field strength, a principle we denote "orientation before destruction."

Place, publisher, year, edition, pages
Cell Press, 2021. Vol. 120, no 17, p. 3709-3717, article id S0006-3495(21)00603-2
National Category
Biophysics
Research subject
Chemistry with specialization in Biophysics
Identifiers
URN: urn:nbn:se:uu:diva-449970DOI: 10.1016/j.bpj.2021.07.017ISI: 000697106900018PubMedID: 34303701OAI: oai:DiVA.org:uu-449970DiVA, id: diva2:1592569
Funder
EU, Horizon 2020, 801406Knut and Alice Wallenberg FoundationSwedish Research Council, 2018-00740Carl Tryggers foundation Swedish National Infrastructure for Computing (SNIC), SNIC 2020/15-67Swedish National Infrastructure for Computing (SNIC), SNIC 2019/8-314Swedish National Infrastructure for Computing (SNIC), 2019/30-47Available from: 2021-09-09 Created: 2021-09-09 Last updated: 2024-01-15Bibliographically approved

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Sinelnikova, AnnaMandl, ThomasAgelii, HaraldGrånäs, OscarMarklund, ErikCaleman, Carl

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Sinelnikova, AnnaMandl, ThomasAgelii, HaraldGrånäs, OscarMarklund, ErikCaleman, CarlDe Santis, Emiliano
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Materials TheoryChemical and Bio-Molecular PhysicsDepartment of Physics and AstronomyBiochemistryMolecular biophysicsScience for Life Laboratory, SciLifeLab
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