Albumin conformational flexibility

A high degree of conformational flexibility of albumin has been recog-... 

Mn ", Co ", and Ni (Friedberg, 1975). The remarkable affinity of serum albumin for the binding of these various ligands is accounted for by its unusual ability to exhibit subtle conformational flexibility of the molecule (Karush, 1950 Foster, 1960). Albumin from either human, bovine, or rabbit was shown to be essential and can replace serum or plasma for growth of stimulated lymphocytes (Spieker-Polet and Polet,... 

For example, Kiosseoglou [75] discussed the role of surface-active lipids at the O/W interface on the viscoelastic parameters of bovine serum albumin (BSA), sodium caseinate, and egg yolk films during adsorption at the olive oil/ protein solution interface. It was postulated that film viscoelasticity was the result of the interaction of surface-active lipids with folded and unfolded proteins at the interface. Benjamins et al. [76] were the first to report on the development of interfacial viscoelasticity at the O/W interface. They found that the proteins with the least conformational flexibility increased the interfacial viscoelastic modulus the most (ovalbumin > BSA > sodium caseinate). 

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