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- W2084301904 abstract "The stability parameters ΔGst, ΔHst and ΔSst of native basic pancreatic trypsin inhibitor (BPTI) have been characterized by microcalorimetric unfolding studies in various buffer solutions, at different pH values and in the presence of guanidine hydrochloride. The unfolding enthalpy of BPTI, in contrast to other globular proteins, exhibits a very small dependence on temperature, which results in a characteristic different temperature dependence of the Gibbs energy of stabilization. BPTI has a very high specific Gibbs energy of stabilization, which renders the slow exchange rates of amide protons understandable. Comparison of the unfolding entropy of BPTI at 110°C with corresponding values of other proteins, revealed that the ΔS values of BPTI are lower by 2·9 J/(K · residue). This lower value of the unfolding entropy is in good agreement with predictions of a theoretical study by Poland & Scheraga (1965) where the influence of crosslinks on the configurational entropy has been studied. Additionally, we were able to calculate an interaction enthalpy per site of −5·6 kJ/mol based on the measurements of unfolding of BPTI in 6 m-guanidine hydrochloride." @default.
- W2084301904 created "2016-06-24" @default.
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- W2084301904 date "1983-11-01" @default.
- W2084301904 modified "2023-09-30" @default.
- W2084301904 title "Basic pancreatic trypsin inhibitor has unusual thermodynamic stability parameters" @default.
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- W2084301904 doi "https://doi.org/10.1016/s0022-2836(83)80130-2" @default.
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