Ligand binding and pH influence conformational flexibility of domains I and III in bovine serum albumin

Bovine Serum Albumin (BSA) is a multi-functional protein that changes its conformation in response to pH and has a high binding capacity for various ligands. Due to these properties, BSA can be used in immunoassay and cell culture applications. To understand how BSA may affect assay function, it is important to understand the flexibility and dynamics of BSA and how it can influence these applications. BSA is a 66-kDa protein composed of three structurally homologous domains. Ligand binding sites can be affected by change in pH as it nears the isoelectric point 4.7-5.2.