Effect of osmoregulatory solutes on the stability of proteins

Gopal, Swarita ; Ahluwalia, Jagdish C. (1993) Effect of osmoregulatory solutes on the stability of proteins Journal of the Chemical Society, Faraday Transactions, 89 (15). pp. 2769-2774. ISSN 0300-9599

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Official URL: http://www.rsc.org/publishing/journals/FT/article....

Related URL: http://dx.doi.org/10.1039/FT9938902769


The thermal denaturation of ribonuclease A and lysozyme in aqueous solutions of osmoregulatory solutes methylamines [trimethylamine N-oxide, betaine (trimethylammonioacetate) and sarcosine] and urea have been investigated by differential scanning calorimetry (DSC). The transition temperature, heat capacity and enthalpy of denaturation in aqueous solutions of ribonuclease A and lysozyme at pH 6.00 have been determined by a least-squares fit of the excess heat capacity data to the two-state model. Thermodynamic functions of denaturation, ΔG°, ΔH° and ΔS° at various temperatures have also been evaluated. The methylamines increase the thermal stability of ribonuclease A and lysozyme in the order : trimethylamine N-oxide > sarcosine > betaine. The stabilizing effect of methylamines when compared with that of amino acids follows the order : trimethylamine N-oxide > glycine > β-alanine > gamma-aminobutyric acid > sarcosine > serine > α-alanine > betaine > proline. The structure-stabilizing effect of methylamines and structure-destabilizing effect of urea on ribonuclease A are nearly additive. No net effect on the stability of ribonuclease A is observed in a 2 :1 mixture of urea and methylamines.

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