http://www.cnr.it/ontology/cnr/individuo/prodotto/ID13934
Thermodynamics of azurin folding: the role of the copper ion (Articolo in rivista)
- Type
- Label
- Thermodynamics of azurin folding: the role of the copper ion (Articolo in rivista) (literal)
- Anno
- 2008-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1007/s10973-007-8422-z (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- M. Pappalardo;1* M. F. M. Sciacca;1 D. Milardi;2 D. M. Grasso;1 and C. La Rosa;1 (literal)
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
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- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- 1Dipartimento di Scienze Chimiche, Universit? di Catania, V.le A. Doria 6, 95125 Catania, Italy
2Istituto di Biostrutture e Bioimmagini, CNR, Sezione di Catania, Viale Andrea Doria 6, 95125 Catania, Italy (literal)
- Titolo
- Thermodynamics of azurin folding: the role of the copper ion (literal)
- Abstract
- 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 degrees 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. (literal)
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