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 degrees C. Study holds ProTherm entries: 20618, 20619, 20620, 20621, 20622, 20623, 20624, 20625, 20626, 20627, 20628, 20629, 20630, 20631, 20632, 20633, 20634, 20635, 20636, 20637, 20638, 20639, 20640, 20641, 20642, 20643, 20644, 20645, 20646, 20647, 20648, 20649, 20650, 20651, 20652, 20653, 20654, 20655, 20656, 20657, 20658, 20659, 20660, 20661, 20662 Extra Details: Protein stability; Guanidinium chloride denaturation; Enzyme activity; Polyol osmolytes; Lysozyme; Ribonuclease-A

Submission Details

ID: tXmZkqQt

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:53 p.m.

Version: 1

Publication Details

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