Deletion of the terminal sequences from cytochromes c.

A 12-residue helical segment was deleted from the amino terminus of human heart cytochrome c by cleavage with cyanogen bromide. The resultant hemepeptide (13-104)H is rather insoluble in aqueous solution at neutral pH. Analysis of the crystallographic model with the terminal segment removed as well as qualitative spectral analysis of a transiently soluble sample of (13-104)H suggests that the hemepeptide retains little of the conformation of the native protein. By contrast, hemepeptide (1-80)H obtained by deletion of the carboxyl terminus is quite soluble at neutral pH. Spectral and hydrodynamic measurements suggest that the heme is encapsulated in an apolar cluster stabilized in part by axial ligation of the heme iron.