Research & Teaching Faculty

Structure and interaction in aqueous urea-trimethylamine-N-oxide solutions

TitleStructure and interaction in aqueous urea-trimethylamine-N-oxide solutions
Publication TypeJournal Article
Year of Publication2007
AuthorsPaul, S, Patey, GN
JournalJournal of the American Chemical Society
Date PublishedApr
ISBN Number0002-7863

u The structural and energetic properties of solutions containing water, urea, and trimethylamine-N-oxide (TMAO) are examined using molecular dynamics simulations. Such systems are of interest mainly because TMAO acts to counter the protein denaturing effect of urea. Even at relatively high concentration, TMAO is found to fit well into the urea-water structure. The underlying solution structure is influenced by TMAO, but these perturbations tend to be modest. The TMAO-water and TMAO-urea interaction energies make an important contribution to the total energy in solutions where counter-denaturing effects are expected. TMAO-water and TMAO-urea hydrogen bonds have the largest hydrogen-bond energies in the system. Additionally, TMAO cannot hydrogen bond with itself, and hence it interacts strongly with water and urea. These observations suggest that the mechanism of TMAO counter denaturation is simply that water and urea prefer to solvate TMAO rather than the protein, hence inhibiting its unfolding.

URL<Go to ISI>://000245723800063