• Structural changes during the unfolding of Bovine serum albumin in the presence of urea: A small-angle neutron scattering study

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    • Keywords


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

    • Abstract


      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.

    • Author Affiliations


      Amit Das1 R Chitra1 R R Choudhury1 M Ramanadham1

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

  • Pramana – Journal of Physics | News

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