Sulfate anion stabilization of native ribonuclease A both by anion binding and by the Hofmeister effect.


Data are reported for T(m), the temperature midpoint of the thermal unfolding curve, of ribonuclease A, versus pH (range 2-9) and salt concentration (range 0-1 M) for two salts, Na(2)SO(4) and NaCl. The results show stabilization by sulfate via anion-specific binding in the concentration range 0-0.1 M and via the Hofmeister effect in the concentration range… (More)


7 Figures and Tables

Slides referencing similar topics