[Secondary structure of proteins from circular dichroism spectra. V. Secondary structure of proteins in a "molten globule" state].

A method that accounts for the contribution made by aromatic amino acid residues in circular dichroism spectra of proteins has been used in order to analyze the structure of bovine carboanhydrase B, bovine and human alpha-lactalbumin in the native state and when denatured with acid and temperature. At acid- and temperature-induced transitions of the secondary structure of these proteins has been shown not to change. However the rigidity of their tertiary structure decreases (the environment of aromatic amino acid residues is made more symmetrical).