SANS and DLS Studies of Protein Unfolding in Presence of Urea and Surfactant

Journal Article · Mon Mar 17 04:00:00 EDT 2008 · AIP Conference Proceedings

DOI:https://doi.org/10.1063/1.2906093· OSTI ID:21136862

Aswal, V K; Chodankar, S N; Wagh, A G ^[1]; Kohlbrecher, J; Vavrin, R ^[2]

---

1. Solid State Physics Division, Bhabha Atomic Research Centre, Mumbai 400085 (India)
2. Laboratory for Neutron Scattering, ETH Zurich and Paul Scherrer Institut, CH-5232 Villigen PSI (Switzerland)

Small-angle neutron scattering (SANS) and dynamic light scattering (DLS) have been used to study conformational changes in protein bovine serum albumin (BSA) during its unfolding in presence of protein denaturating agents urea and surfactant. On addition of urea, the BSA protein unfolds for urea concentrations greater than 4 M and acquires a random coil configuration with its radius of gyration increasing with urea concentration. The addition of surfactant unfolds the protein by the formation of micelle-like aggregates of surfactants along the unfolded polypeptide chains of the protein. The fractal dimension of such a protein-surfactant complex decreases and the overall size of the complex increases on increasing the surfactant concentration. The conformation of the unfolded protein in the complex has been determined directly using contrast variation SANS measurements by contrast matching the surfactant to the medium. Results of DLS measurements are found to be in good agreement with those obtained using SANS.

• OSTI ID: 21136862
• Journal Information: AIP Conference Proceedings, Journal Name: AIP Conference Proceedings Journal Issue: 1 Vol. 989; ISSN 0094-243X; ISSN APCPCS
• Country of Publication: United States
• Language: English

Related Subjects

37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
ALBUMINS
BIOPHYSICS
CONFORMATIONAL CHANGES
CRYSTALLOGRAPHY
LIGHT SCATTERING
MOLECULAR STRUCTURE
NEUTRON DIFFRACTION
POLYPEPTIDES
SMALL ANGLE SCATTERING
SURFACTANTS
UREA
VARIATIONS