Dipartimento di Scienze Chimiche, Universit di Catania, V. le A. Doria 6, Catania 95125, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Sezione di Catania, Viale Andrea Doria 6, Catania 95125, Italy
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Smith, R.M., Martell, A.E., (1989) Critical Stability Constants: Volume 6 Second Supplement, , Plenum Press New York and London
Thermodynamics Of Azurin Folding: The Role Of The Copper Ion
The role played by the metal ion in thermodynamics of azurin folding was addressed by studying the thermal denaturation of the apo-form by differential scanning calorimetry (DSC), and by comparing the results with data concerning the holo protein. The thermal unfolding experiments showed that at 25 C the presence of metal ion increases the thermodynamic stability of azurin by 24 kJ mol-1. A comparison between the unfolding and the copper binding free energies allow us to assert that the unfolded polypeptide chain binds copper and subsequently folds into native holo azurin, being this the thermodynamically most favourable process in driving azurin folding. 2008 Springer Science+Business Media, LLC
Thermodynamics Of Azurin Folding: The Role Of The Copper Ion
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Thermodynamics Of Azurin Folding: The Role Of The Copper Ion