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Testing polyols’ compatibility with Gibbs energy of stabilization of proteins under conditions in which they behave as compatible osmolytes
Author(s) -
Haque Inamul,
Singh Rajendrakumar,
Ahmad Faizan,
Moosavi-Movahedi Ali Akbar
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.06.005
Subject(s) - osmolyte , chemistry , lysozyme , denaturation (fissile materials) , sorbitol , glycerol , ribonuclease , guanidinium chloride , native state , gibbs free energy , polyol , ectoine , osmoprotectant , protein folding , xylitol , biochemistry , thermodynamics , enzyme , organic chemistry , proline , nuclear chemistry , amino acid , rna , physics , fermentation , polyurethane , gene
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.