Click here to view fulltext PDF

Permanent link:
https://www.ias.ac.in/article/fulltext/pram/063/02/0363-0368

Small-angle neutron scattering; Bovine serum albumin; urea denaturation

The native form of serum albumin is the most important soluble protein in the body plasma. In order to investigate the structural changes of Bovine serum albumin (BSA) during its unfolding in the presence of urea, a small-angle neutron scattering (SANS) study was performed. The scattering curves of dilute solutions of BSA with different concentrations of urea in D₂O at pH 7.2 ± 0.2 were measured at room temperature. The scattering profile was fitted to a prolate ellipsoidal shape (a, b, b) of the protein witha = 52.2 Å andb = 24.2 Å. The change in the dimensions of the protein as it unfolds was found to be anisotropic. The radius of gyration of the compact form of the protein in solution decreased as the urea concentration was increased.

Amit Das¹ R Chitra¹ R R Choudhury¹ M Ramanadham¹

1. Solid State Physics Division, Bhabha Atomic Research Centre, Mumbai - 400 085, India

Published

August 2004