Related Experiment Video
Updated: Feb 5, 2026

Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of GoldIII
Published on: August 31, 2018
INTERMOLECULAR INTERACTIONS IN THE SOLUTIONS OF SERUM ALBUMIN
Abstract:
The mechanisms of intermolecular protein complex formation were studied by the example of monomers, oligomers and aggregates of bovine serum albumin (BSA) depending on the protein concentration, pH and urea concentration. Using dynamic light scattering (DLS), analytical ultracentrifugation (AUC) and PAG electrophoresis, we have shown that there is dynamic equilibrium between monomers and aggregates in BSA solution. Decreasing pH of the solution (4.0—1.0) resulted in increasing sizes of the aggregates. In the solutions with low urea concentrations (below 2 M), the sizes of aggregates decreased, while higher urea concentrations induced formation of larger aggregates due to the unfolding of the protein.
Related Concept Videos
Intermolecular Forces in Solutions
When the strengths of the intermolecular forces of attraction between solute and solvent species in a solution are no different than those present in the separated components, the solution is formed with no accompanying energy change. Such a solution is called an ideal solution. A mixture of ideal gases (or gases such as helium and argon,...
Intermolecular Forces
Intermolecular vs Intramolecular Forces
Ideal Solutions
Comparing Intermolecular Forces: Melting Point, Boiling Point, and Miscibility
Temporary attractive forces like dispersion are present in all molecules, whether they are polar or nonpolar. They...
Solution Formation
This selective...

