Abstract

Urea induced equilibrium unfolding of fatted and defatted human serum albumin (HSA) showed that fatty acid stabilizes native and intermediate states. Similarly acid induced unfolding of fatted and defatted HSA also showed that fatty acid stabilizes NF and FE transitions. These results also showed that five electrostatic interactions along with one buried carboxyl group of acidic amino acid are involved in acid induced unfolding of HSA.

Keywords: Acid induced unfolding, conformational stability, hydrodynamic volume, intrinsic viscosity, urea induced unfolding