Electronic fluctuation in physiological solutions: Trimethylamine N-oxide and tert-butyl alcohol

20 April 2022, Version 1
This content is a preprint and has not undergone peer review at the time of posting.

Abstract

Although small organic molecules in cells have been considered important to control the functions of proteins, their electronic fluctuation under real physiological conditions has never been clarified due to the lack of observations. Herein, the time evolutions of the interactions in dilute aqueous trimethylamine N-oxide (TMAO) and tert-butyl alcohol (TBA) solutions were analyzed via ab initio molecular dynamics simulations accelerated with the fragment molecular theory. It has been known that TMAO and TBA have similar structures, but opposite physiological functions to stabilize and destabilize proteins. It was clarified that water dipole in the TMAO solutions are up to 1.5 times enhanced that affect protein stabilization. Understanding the solution dynamics will contribute to artificial chaperone design in next generation medicine.

Supplementary materials

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Title
Electronic fluctuation in physiological solutions: Trimethylamine N-oxide and tert-butyl alcohol
Description
Supplementary methods, chemical structures, and simulation results on monomers, dimers, and dilute aqueous solution systems (PDF).
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