Individual and combined effects of urea and trimethylamine N-oxide (TMAO) on protein structures

Document Type

Article

Publication Date

11-1-2019

Abstract

In this manuscript, we perform all-atom molecular dynamics simulations of model peptides to study the molecular mechanisms accounting for individual and combined effects of two osmolytes, i.e., urea and trimethylamine N-oxide (TMAO). We find that urea, which is a denaturant osmolyte, destabilizes mainly hydrophobic and intra-backbone interactions. TMAO, which is a protecting osmolyte, stabilizes charge-charge and intra-backbone interactions whereas it destabilizes hydrophobic interactions. We show that charge-charge interactions are highly sensitive to the presence of TMAO and it may be the main interaction accounting for TMAO stabilizing effect on proteins. These charge-charge interactions are also shown to play a dominant role in how TMAO counteracts the effect of urea. These results are rationalized in terms of the preferential interaction of osmolytes.

Identifier

85070259489 (Scopus)

Publication Title

Journal of Molecular Liquids

External Full Text Location

https://doi.org/10.1016/j.molliq.2019.111443

ISSN

01677322

Volume

293

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