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 articlepeer-review

23 Citations (Scopus)

Abstract

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
Volume19
Issue number10
DOIs
Publication statusPublished - 2017

All Science Journal Classification (ASJC) codes

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

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