Testing polyols’ compatibility with Gibbs energy of stabilization of proteins under conditions in which they behave as compatible osmolytes | Zendy

Haque Inamul | Zendy; Singh Rajendrakumar | Zendy; Ahmad Faizan | Zendy; Moosavi-Movahedi Ali Akbar | Zendy

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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.

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