The role played by the α-helix in the unfolding pathway and stability of azurin: Switching between hierarchic and nonhierarchic folding(311 views) Manetto GD, Grasso DM, Milardi D, Pappalardo M, Guzzi R, Sportelli L, Verbeet MP, Canters GW, La Rosa C
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2007 Nov 5; 8(16): 1941-1949.
Keywords: Azurin, Protein Folding, Protein Structures, Site-Directed Mutagenesis, Thermodynamic Stability, Alpha Helix, Article, Fluorescence Microscope, Nuclear Magnetic Resonance Spectroscopy, Priority Journal, Protein Function, Protein Stability, Proteomics, Thermostability, Kinetics, Models, Molecular, Oxidation-Reduction, Protein Denaturation, Secondary, Reference Standards, Temperature,
Affiliations: *** IBB - CNR ***
Dipartimento di Scienze Chimiche, Università di Catania, Viale A. Doria 6, 95125 (CT), Italy
Istituto di Biostrutture e Bioimmagini, Consiglio Nazionale Delle Ricerche, Viale A. Doria 6, 95125 (CT), Italy
Dipartimento di Fisica, Università Della Calabria, 87030 Rende (CS), Italy
Leiden Institute of Chemistry, Gorleaus Laboratories, Leiden University, P.O. Box 9502, 2300 RA Leiden, Netherlands
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The role played by the α-helix in the unfolding pathway and stability of azurin: Switching between hierarchic and nonhierarchic folding