Abstract DSC measurements have been accomplished in aqueous solutions of bovine pancreatic ribonuclease A (RNAase A) in the presence of subsaturating amounts of 3′ cytidine monophosphate (3′ CMP) and 2′ cytidine monophosphate (2′ CMP) atpH 5.0 and 5.5. In these conditions the experimental profiles do not conform to a one-step unfolding process. It can be emphasized, as a general phenomenon, that a strong linkage between the temperature-induced protein unfolding and the ligand binding, when the ligand is less than the saturation level, causes marked distortions from a two-state transition. A purely equilibrium thermodynamic analysis gives a correct account of this behaviour and allows to simulate calorimetric curves. It is thus possible to obtain, in an indirect manner, information about the thermodynamic parameters concerning the binding process, namely the association constant and the binding enthalpy. The values ofKb and Δb H for 3′CMP and 2′CMP, so determined, are consistent with the literature data.

Ligand-induced biphasic thermal denaturation of RNase A / G., Barone; DEL VECCHIO, POMPEA GIUSEPPINA GRAZIA; D., Fessas; Giancola, Concetta; G., Graziano; A., Riccio. - In: JOURNAL OF THERMAL ANALYSIS. - ISSN 0368-4466. - STAMPA. - 41:(1994), pp. 1263-1276. [10.1007/BF02549921]

Ligand-induced biphasic thermal denaturation of RNase A.

DEL VECCHIO, POMPEA GIUSEPPINA GRAZIA;GIANCOLA, CONCETTA;
1994

Abstract

Abstract DSC measurements have been accomplished in aqueous solutions of bovine pancreatic ribonuclease A (RNAase A) in the presence of subsaturating amounts of 3′ cytidine monophosphate (3′ CMP) and 2′ cytidine monophosphate (2′ CMP) atpH 5.0 and 5.5. In these conditions the experimental profiles do not conform to a one-step unfolding process. It can be emphasized, as a general phenomenon, that a strong linkage between the temperature-induced protein unfolding and the ligand binding, when the ligand is less than the saturation level, causes marked distortions from a two-state transition. A purely equilibrium thermodynamic analysis gives a correct account of this behaviour and allows to simulate calorimetric curves. It is thus possible to obtain, in an indirect manner, information about the thermodynamic parameters concerning the binding process, namely the association constant and the binding enthalpy. The values ofKb and Δb H for 3′CMP and 2′CMP, so determined, are consistent with the literature data.
1994
Ligand-induced biphasic thermal denaturation of RNase A / G., Barone; DEL VECCHIO, POMPEA GIUSEPPINA GRAZIA; D., Fessas; Giancola, Concetta; G., Graziano; A., Riccio. - In: JOURNAL OF THERMAL ANALYSIS. - ISSN 0368-4466. - STAMPA. - 41:(1994), pp. 1263-1276. [10.1007/BF02549921]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/139883
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