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Reproducibility in the unfolding process of protein induced by an external electric field.

ABSTRACT: The dynamics of proteins are crucial for their function. However, commonly used techniques for studying protein structures are limited in monitoring time-resolved dynamics at high resolution. Combining electric fields with existing techniques to study gas-phase proteins, such as single particle imaging using free-electron lasers and gas-phase small angle X-ray scattering, has the potential to open up a new era in time-resolved studies of gas-phase protein dynamics. Using molecular dynamics simulations, we identify well-defined unfolding pathways of a protein, induced by experimentally achievable external electric fields. Our simulations show that strong electric fields in conjunction with short-pulsed X-ray sources such as free-electron lasers can be a new path for imaging dynamics of gas-phase proteins at high spatial and temporal resolution.

SUBMITTER: Sinelnikova A

PROVIDER: S-EPMC8179335 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature

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Reproducibility in the unfolding process of protein induced by an external electric field.

Sinelnikova Anna A Mandl Thomas T Östlin Christofer C Grånäs Oscar O Brodmerkel Maxim N MN Marklund Erik G EG Caleman Carl C

Chemical science 20201226 6

The dynamics of proteins are crucial for their function. However, commonly used techniques for studying protein structures are limited in monitoring time-resolved dynamics at high resolution. Combining electric fields with existing techniques to study gas-phase proteins, such as single particle imaging using free-electron lasers and gas-phase small angle X-ray scattering, has the potential to open up a new era in time-resolved studies of gas-phase protein dynamics. Using molecular dynamics simul ...[more]

PMID: 34163965

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