Thermodynamic analysis of the contributions of the copper ion and the disulfide bridge to azurin stability: Synergism among multiple depletions(468 views) Milardi D, Grasso DM, Verbeet MP, Canters GW, La Rosa C
Keywords: Azurin, Copper, Differential Scanning Calorimetry, Disulfide Bridge, Stability, Apo Azurin, Apo Azurin C26 A, Apo Azurin C3 A, Apolipoprotein, Apolipoprotein C26 A, Apolipoprotein C3 A, Copper Ion, Copper Protein, Cysteine, Holo Azurin, Holo Azurin C26 A, Holo Azurin C3 A, Mutant Protein, Unclassified Drug, Amino Acid Substitution, Article, Comparative Study, Depletion, Parameter, Priority Journal, Protein Folding, Protein Stability, Temperature, Thermodynamics, Energy Transfer, Escherichia Coli, Models, Chemical, Mutagenesis, Site-Directed, Protein Conformation, Protein Denaturation, Protein Engineering,
Affiliations: *** IBB - CNR ***
Ist. Biostrutture e Bioimmagini-CNR, Sezione di Catania, Viale Andrea Doria 6, 95125 Catania, Italy
Dipartimento di Scienze Chimiche, Universita' di Catania, Viale Andrea Doria 6, 95125 Catania, Italy
Gorleaus Laboratories, Leiden Institute of Chemistry, Leiden University, P.O. Box 9502, 2300 RA Leiden, Netherlands
References: Not available.
Thermodynamic analysis of the contributions of the copper ion and the disulfide bridge to azurin stability: Synergism among multiple depletions