2018年12月1日 · Herein, the primary structure of BSA was analyzed by SDS-PAGE, secondary structure by Circular Dichroism (CD), and tertiary structure by Fluorescence and SAXS spectroscopy. The zeta-potential measurements shed light …

Small angle scattering (SAS) of X-ray and neutrons provides structural information on biological macromolecules in solution at a resolution of 1-2 nm.

2023年10月18日 · Biological solution SAXS (BioSAXS) is routinely employed at synchrotrons to study biological molecules in solution to determine the scattering form factors and intermolecular...

2006年12月10日 · We have studied a series of samples of bovine serum albumin (BSA) solutions with protein concentration, c, ranging from 2 to 500 mg/mL and ionic strength, I, from 0 to 2 M by small-angle X-ray scattering (SAXS).

2023年3月24日 · Here, we present a novel analytical method using small-angle X-ray scattering (SAXS) to solve the structure of bovine serum albumin (BSA) while encapsulated within two zeolitic imidazolate frameworks (ZIF-67 and ZIF-8).

2016年7月1日 · Protein folded/unfolded states can be detected by SAXS and fluorescence experiments. The pH and the ionic strength affect the apparent molecular weight of the BSA. The BSA in E-form can bind more hydrophobic molecules than in N-form. FL and ITC methods provides correct thermodynamic data for the BSA/ligand interactions.

2003年6月15日 · Classical parameters obtained from surface tension technique coupled to small angle X-ray scattering (SAXS) measurements gave support to investigate conformational changes in the bovine serum albumin (BSA)-sodium dodecyl sulfate (SDS) complexes, as well as the size of the micelle-like clusters distr …

Thermal-induced conformational changes and protein–protein interactions of bovine serum albumin (BSA) in aqueous solution are assessed by small angle X-ray scattering (SAXS) at two pH values (7.4 and 9.0) and two ionic strengths (0.1 and 0.5). We demonstrate that Guinier analysis in two ranges of the modulus

2007年1月11日 · We have studied a series of samples of bovine serum albumin (BSA) solutions with protein concentration, c, ranging from 2 to 500 mg/mL and ionic strength, I, from 0 to 2 M by small-angle X-ray scattering (SAXS). The scattering intensity distribution was compared to simulations using an oblate ellips …

In this work, by using SAXS on BSA as a model system, we have systematically studied the effect of ionic strength on the protein-protein interaction using a large range of salt and protein concentrations. BSA is a globular protein, which is readily soluble in water and stable over a wide range of salt and protein concentrations.