title: Unfolding process of rusticyanin: evidence of protein aggregation.
abstract: The unfolding process of the Blue Copper Protein (BCP) rusticyanin (Rc) has been studied using a wide variety of biochemical techniques. Fluorescence and CD spectroscopies reveal that the copper ion plays an essential role in stabilizing the protein and that the oxidized form is more efficient than the reduced species in this respect. The addition of guanidinium chloride to Rc samples produces aggregation of the protein. Gel filtration chromatography and glutaraldehyde cross-linking experiments confirm the formation of such aggregates. Among the BCPs, this feature is exclusive to Rc. The aggregation could be related to the large molecular mass and large number of hydrophobic residues of this protein compared with those of other BCPs.
authors.affiliation: Instituto de Biología Molecular y Celular, Universidad Miguel Hernández, Spain.
authors.forename: Luis A
authors.initials: LA
authors.lastname: Alcaraz
authors.forename: Antonio
authors.initials: A
authors.lastname: Donaire
mesh_terms: D001400:Azurin / Q000031:analogs & derivatives* / Q000737:chemistry*; D002850:Chromatography, Gel; D002942:Circular Dichroism; D003300:Copper; D003432:Cross-Linking Reagents / Q000494:pharmacology; D004058:Diffusion; D004305:Dose-Response Relationship, Drug; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000378:metabolism; D019791:Guanidine / Q000494:pharmacology; D007477:Ions; D009682:Magnetic Resonance Spectroscopy; D008667:Metalloproteins / Q000737:chemistry; D008958:Models, Molecular; D010100:Oxygen / Q000737:chemistry; D010957:Plasmids / Q000378:metabolism; D011485:Protein Binding; D017510:Protein Folding; D011994:Recombinant Proteins / Q000378:metabolism; D013050:Spectrometry, Fluorescence
chemical_list: D003432:Cross-Linking Reagents; D007477:Ions; D008667:Metalloproteins; D011994:Recombinant Proteins; C012543:rusticyanin; D001400:Azurin; D003300:Copper; D019791:Guanidine; D010100:Oxygen