Differential scanning calorimetry can be used as an interesting tool to study protein-ligand interactions, with the aid of suitable thermodynamic models. This review analyzes and discusses results recently obtained in our laboratory with regard to the binding equilibrium of 2' and 3' cytidine monophosphate to RNAase A, the interaction of S-peptide with S-protein, the binding of D-glucose to yeast hexokinase and the thermal stability of respective complexes.
Differential scanning calorimetry as a tool of study protein-ligand interactions / Barone, G.; Catanzano, F.; DEL VECCHIO, POMPEA GIUSEPPINA GRAZIA; Giancola, C.; Graziano, G.. - In: PURE AND APPLIED CHEMISTRY. - ISSN 0033-4545. - STAMPA. - 67:(1995), pp. 1867-1872.
Differential scanning calorimetry as a tool of study protein-ligand interactions.
DEL VECCHIO, POMPEA GIUSEPPINA GRAZIA;C. GIANCOLA;
1995
Abstract
Differential scanning calorimetry can be used as an interesting tool to study protein-ligand interactions, with the aid of suitable thermodynamic models. This review analyzes and discusses results recently obtained in our laboratory with regard to the binding equilibrium of 2' and 3' cytidine monophosphate to RNAase A, the interaction of S-peptide with S-protein, the binding of D-glucose to yeast hexokinase and the thermal stability of respective complexes.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
