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

Pramana

Amit Das1¹  M Ramanadham¹  R Chitra¹  R R Choudhury¹ 

[1] Solid State Physics Division, Bhabha Atomic Research Centre, Mumbai 400 085, India$$

关键词: Small-angle neutron scattering;    Bovine serum albumin;    urea denaturation.;   

DOI  :  

学科分类：物理（综合）

来源: Indian Academy of Sciences

【 摘 要 】

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 with 𝑎 = 52.2 Å and 𝑏 = 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.

【 授权许可】

Unknown