Thermodynamic analysis of the contributions of the copper ion and the disulfide bridge to azurin stability: synergism among multiple depletions. (Articolo in rivista)

Type

• Articolo in rivista (Classe)
• Prodotto della ricerca (Classe)

Label

• Thermodynamic analysis of the contributions of the copper ion and the disulfide bridge to azurin stability: synergism among multiple depletions. (Articolo in rivista) (literal)

Anno

• 2003-01-01T00:00:00+01:00 (literal)

Alternative label

• Milardi, Danilo; Grasso, Domenico M.; Verbeet, Martin Ph.; Canters, Gerard W.; La Rosa, Carmelo. (2003)
  Thermodynamic analysis of the contributions of the copper ion and the disulfide bridge to azurin stability: synergism among multiple depletions.
  in Archives of biochemistry and biophysics (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Milardi, Danilo; Grasso, Domenico M.; Verbeet, Martin Ph.; Canters, Gerard W.; La Rosa, Carmelo. (literal)

Pagina inizio

• 121 (literal)

Pagina fine

• 127 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 414 (literal)

Rivista

• Archives of biochemistry and biophysics (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali

• 8 (literal)

Note

• ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Milardi, Danilo; Grasso, Domenico M.; La Rosa, Carmelo, Dipartimento di Scienze Chimiche, Università di Catania. Verbeet, Martin Ph.; Canters, Gerard W. University of Leiden, The netherlands. (literal)

Titolo

• Thermodynamic analysis of the contributions of the copper ion and the disulfide bridge to azurin stability: synergism among multiple depletions. (literal)

Abstract

• The stabilizing potential of the copper ion and the disulfide bridge in azurin has been explored with the aim of inspecting the ways in which these two factors influence one another. Specifically, whether copper and disulfide contributions to protein stability are additive has been examd. To this aim, the thermal unfolding of a copper-depleted mutant lacking the disulfide bridge between Cys3 and Cys26 (apo C3A/C26A azurin) was studied by differential scanning calorimetry. A comparison of the unfolding parameters of holo and apo C3A/C26A azurin with the apo C3A/C26A protein has shown that the effects of simultaneous copper and disulfide depletion are additive only at two temps.: T=15° and T=67°. Within this range the presence of the copper ion and the disulfide bridge has a pos. synergistic effect on azurin stability. These findings might have implications for the rational use of the stabilizing potential of copper and disulfides in copper protein engineering (literal)

Prodotto di

• Institute of biostructure and bioimaging (IBB) (Istituto)

Autore CNR

• DANILO MILARDI (Unità di personale interno)

Incoming links:

Autore CNR di

• DANILO MILARDI (Unità di personale interno)

Prodotto

• Institute of biostructure and bioimaging (IBB) (Istituto)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Archives of biochemistry and biophysics (Rivista)