Contributions of polar and apolar groups to the thermodynamic stability of azurin |
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Authors: | D Milardi S Fasone C La Rosa D Grasso |
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Institution: | (1) Dipartimento di Scienze Chimiche, Viale Andrea Doria 6, 95125 Catania, Italy |
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Abstract: | Summary All denaturational thermodynamic changes (ΔH, ΔS, ΔG) were calculated for the thermal unfolding of azurin fromPseudomonas Aeruginosa. DSC data could not be directly studied in terms of classical thermodynamics, because the thermal unfolding of azurin is
an irreversible process. However, a mathematical extrapolation of heat capacity curves to infinite scan rate allowed us to
obtain the denaturational enthalpy change and the melting temperature related to the reversible step. The denaturational heat
capacity change (ΔC
p
), together with all the relevant contributions of polar and apolar groups to the thermodynamic parameters of azurin were
calculated according to an approach taking into account the common features of protein unfolding and dissolution of model
compounds. A comparison between the experimental and the expected denaturational thermodynamic values was briefly discussed. |
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Keywords: | Molecular biophysics |
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