Ontology highlight
ABSTRACT:
SUBMITTER: Bennion BJ
PROVIDER: S-EPMC404062 | biostudies-literature | 2004 Apr
REPOSITORIES: biostudies-literature
Bennion Brian J BJ Daggett Valerie V
Proceedings of the National Academy of Sciences of the United States of America 20040419 17
Proteins are very sensitive to their solvent environments. Urea is a common chemical denaturant of proteins, yet some animals contain high concentrations of urea. These animals have evolved an interesting mechanism to counteract the effects of urea by using trimethylamine N-oxide (TMAO). The molecular basis for the ability of TMAO to act as a chemical chaperone remains unknown. Here, we describe molecular dynamics simulations of a small globular protein, chymotrypsin inhibitor 2, in 8 M urea and ...[more]