Elucidation of μs dynamics of domain-III of human serum albumin during the chemical and thermal unfolding: A fluorescence correlation spectroscopic investigation
Denaturation of domain-III of HSA is studied by covalent marker for the first time. Global and domain-III denaturation were found to follow different pathways. Intermediate state/s during the denaturation is detected within the domain-III. Effects of GnHCl and heat on domain-III of HSA are found to be different. Conformational dynamics during the course of denaturation has been elucidated.