Molecular Mechanism for the Hofmeister Effect Derived from NMR and DSC Measurements on Barnase.

ABSTRACT: The effects of sodium thiocyanate, sodium chloride, and sodium sulfate on the ribonuclease barnase were studied using differential scanning calorimetry (DSC) and NMR. Both measurements reveal specific and saturable binding at low anion concentrations (up to 250 mM), which produces localized conformational and energetic effects that are unrelated to the Hofmeister series. The binding of sulfate slows intramolecular motions, as revealed by peak broadening in ¹³C heteronuclear single quantum coherence spectroscopy. None of the anions shows significant binding to hydrophobic groups. Above 250 mM, the DSC results are consistent with the expected Hofmeister effects in that the chaotropic anion thiocyanate destabilizes barnase. In this higher concentration range, the anions have approx

SUBMITTER: Bye JW 

PROVIDER: S-EPMC6640789 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature