UREA- AND THERMAL-INDUCED UNFOLDING OF BOVINE SERUM ALBUMIN

Abstract

In this work, the difference between pH-induced isomerization and urea-induced unfolding, and the urea- and thermal-induced unfolding processes in different isomeric forms of Bovine serum albumin (BSA) are studied experimentally. Our results show that urea-induced unfolding is a two-step, three-state transition in both the N-form and the B-form, but a single-step, two-state transition in both the E-form and the F-form. At the same time, thermal-induced unfolding shows a two-state transition in all isomeric forms, but the cooperativity of unfolding is different.