Trimethylamine-N-oxide: Its hydration structure, surface activity, and biological function, viewed by vibrational spectroscopy and molecular dynamics simulations

Tatsuhiko Ohto, Johannes Hunger, Ellen H.G. Backus, Wataru Mizukami, Mischa Bonn, Yuki Nagata

    Research output: Contribution to journalReview article

    19 Citations (Scopus)


    The osmolyte molecule trimethylamine-N-oxide (TMAO) stabilizes the structure of proteins. As functional proteins are generally found in aqueous solutions, an important aspect of this stabilization is the interaction of TMAO with water. Here, we review, using vibrational spectroscopy and molecular dynamics simulations, recent studies on the structure and dynamics of TMAO with its surrounding water molecules. This article ends with an outlook on the open questions on TMAO-protein and TMAO-urea interactions in aqueous environments.

    Original languageEnglish
    Pages (from-to)6909-6920
    Number of pages12
    JournalPhysical Chemistry Chemical Physics
    Issue number10
    Publication statusPublished - Jan 1 2017


    All Science Journal Classification (ASJC) codes

    • Physics and Astronomy(all)
    • Physical and Theoretical Chemistry

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