title: Theoretical study of interactions of BSA protein in a NaCl aqueous solution.
abstract: Bovine Serum Albumine (BSA) aqueous solutions in the presence of NaCl are investigated for different protein concentrations and low to intermediate ionic strengths. Protein interactions are modeled via a charge-screened colloidal model, in which the range of the potential is determined by the Debye-Hückel constant. We use Monte Carlo computer simulations to calculate the structure factor, and assume an oblate ellipsoidal form factor for BSA. The theoretical scattered intensities are found in good agreement with the experimental small angle X-ray scattering intensities available in the literature. The performance of well-known integral equation closures to the Ornstein-Zernike equation, namely the mean spherical approximation, the Percus-Yevick, and the hypernetted chain equations, is also assessed with respect to computer simulation.
authors.affiliation: School of Chemistry and Physics, University of KwaZulu-Natal Private Bag X01, Scottsville 3209, Pietermaritzburg, South Africa. pellicane@ukzn.ac.za
authors.forename: Giuseppe
authors.initials: G
authors.lastname: Pellicane
authors.forename: Miguel
authors.initials: M
authors.lastname: Cavero
mesh_terms: D000818:Animals; D002417:Cattle; D003198:Computer Simulation; D008954:Models, Biological; D009010:Monte Carlo Method; D009994:Osmolar Concentration; D053838:Scattering, Small Angle; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism*; D012965:Sodium Chloride / Q000737:chemistry / Q000378:metabolism*; D014961:X-Ray Diffraction
chemical_list: D012710:Serum Albumin, Bovine; D012965:Sodium Chloride