The 26th International Conference on Accelerators and Beam Utilizations

Structurally denatured BSA using small-angle X-ray scattering

Nov 14, 2024, 1:00 PM

1h 30m

2F Poster Hall

Board: WG4-14

Poster ICABU WG4. Applications of Particle Beams ICABU Poster Session

Speaker

Siti Khadijah Maliki (Division of Advanced Nuclear Engineering (DANE), Pohang University of Science and Technology (POSTECH))

Description

We employed small-angle X-ray scattering (SAXS) to investigate the conformational transitions of bovine serum albumin (BSA) across a wide range of urea concentrations (0–8 M). By constructing three-dimensional (3D) ab initio models using GASBOR, we described the structural evolution of BSA from its native state to denatured and unfolded conformations. By integrating size exclusion chromatography and SAXS (SEC-SAXS), we accurately isolated elution profiles corresponding to monomeric BSA, even under conditions of conformational polydispersity at high urea concentrations (5–8 M). Detailed analysis yielded precise measurements of the radius of gyration (Rg) and maximum dimension (Dmax) derived from the pair distance distribution function P(r). Our results revealed that BSA maintains its native conformation at low urea concentrations (0–3 M), undergoes partial denaturation at 4 M urea, and fully unfolds at concentrations of 5–8 M. These findings offer valuable insights into the relationship between structural stability and protein function, contributing to a deeper understanding of protein folding and stability under denaturing conditions.