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- W2028851071 abstract "It is generally believed that compatible osmolytes stabilize proteins by shifting the denaturation equilibrium, native state ↔ denatured state toward the left. We show here that if osmolytes are compatible with the functional activity of the protein at a given pH and temperature, they should not significantly perturb this denaturation equilibrium under the same experimental conditions. This conclusion was reached from the measurements of the activity parameters ( K m and k cat ) and guanidinium chloride‐induced denaturations of lysozyme and ribonuclease‐A in the presence of five polyols (sorbitol, glycerol, mannitol, xylitol and adonitol) at pH 7.0 and 25 °C." @default.
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- W2028851071 date "2005-06-20" @default.
- W2028851071 modified "2023-09-26" @default.
- W2028851071 title "Testing polyols’ compatibility with Gibbs energy of stabilization of proteins under conditions in which they behave as compatible osmolytes" @default.
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- W2028851071 doi "https://doi.org/10.1016/j.febslet.2005.06.005" @default.
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