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.
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