ArticleBiophysical journal2021
Protein orientation in time-dependent electric fields: orientation before destruction.
Article in Biophysical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 25 citations in OpenAlex.
- Biological applications at the AQUA beamline of the EuPRAXIA@SPARC_LAB free electron laser.European biophysics journal : EBJ · 2026Article
- Mass spectrometry integrates protein design into structural biology method development.QRB discovery · 2026Review
- Partial orientation retrieval of proteins from X-ray free-electron-laser induced explosions for single particle imaging.Scientific reports · 2025Article
- High-Performance Molecular Dynamics Simulations for Native Mass Spectrometry of Large Protein Complexes with the Fast Multipole Method.Analytical chemistry · 2024Article
- Article
- Electrochemistry in sensing of molecular interactions of proteins and their behavior in an electric field.Mikrochimica acta · 2023Review
- Coherent diffractive imaging of proteins and viral capsids: simulating MS SPIDOC.Analytical and bioanalytical chemistry · 2023Article
- Rehydration Post-orientation: Investigating Field-Induced Structural Changes via Computational Rehydration.The protein journal · 2023Article
- Stability and conformational memory of electrosprayed and rehydrated bacteriophage MS2 virus coat proteins.Current research in structural biology · 2022Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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."
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.