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• W1487486255 abstract "The conformational transitions of calcium binding protein parvalbumin III from carp muscle were studied by scanning calorimetry, potentiometric titration and isothermal calorimetric titration. Changes of Gibbs energy, enthalpy and partial heat cap city were determined. The removal of calcium ions by EDTA is accompanied by 1) a heat absorption of 75 ± 10 kJ per mole of the protein. 2) a decrease in the Gibbs energy of protein structure stabilisation of about 42 kJ mol−1 and 3) a decrease in thermostability by more than 50 K. The protonation of the acidic groups leads to a loss of calcium followed by denaturation, while the pH of the transition strongly depends on calcium activity. The enthalpy and heat capacity changes at denaturation are comparable with the values observed for other compact globular proteins." @default.
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• W1487486255 date "1978-05-01" @default.
• W1487486255 modified "2023-10-11" @default.
• W1487486255 title "Thermodynamic investigations of proteins" @default.
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• W1487486255 doi "https://doi.org/10.1016/0301-4622(78)80003-9" @default.
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