study of denaturation of human serum albumin

Differential Temperature-Perturbation Spectroscopy shows that the denaturation of Human Serum Albumin [HSA] produces despiralization of the molecule with simultaneous accessibility of tyrosyl residues. The quantity of tyrosyl residues increases with parallel decrease in alpha helics which is determined by the Optical Rotation Dispersion [ORD] in the range of 300-600 nm. On the basis of primary structure of albumin, the orientation of alpha helics along the polypeptide chain has been calculated. It has been shown that the 50% of tyrosyl residues are placed at the ends of the proposed helics. This explains the correlated data obtained with the help of ORD and Differential Perturbation Spectroscopy