A combined scanning dilatometric and differential scanning calorimetric study of the thermal unfolding of bovine serum albumin

Spherical polyelectrolyte brushes as carrier particles for proteins: An investigation of the structure of adsorbed and desorbed bovine serum albumin

“…4, curve A) shows a sigmoidal temperature dependence with a transition region at 60-63 • C which locates the temperature of unfolding of the protein molecules. Using differential scanning calorimetry, the maximum differential heat capacity of a BSA solution at pH = 7 has been found at 62 • C by Grasso and co-workers [40], in very good agreement with the temperature of unfolding observed in our study.…”

Protein detection using aqueous/LC interfaces decorated with a novel polyacrylic acid block liquid crystalline polymer

“…Lysozyme, BSA, a-lactalbumin, and insulin were tested with our TEM grid cell. The pIs of lysozyme, BSA, 21,22 a-lactalbumin, 23,24 and insulin 25,26 are 11.4, 5.3, 4.2, and 5.3, respectively. The respective sizes for these proteins are 14.9, 66.4, 14.2, and 6 kilodalton (kDa).…”

Tuning the selective interaction of lysozyme and serum albumin on a carboxylate modified surface

“…15,20,21 In this article, two different proteins were chosen as model proteins that vary in protein net charge and thermodynamic stability against unfolding, namely, hen egg white lysozyme (pH IEP y 11, DG y 63 kJ mol 21 ) 24,25 and bovine serum albumin (pH IEP y 4.8, DG y 18 kJ mol 21 ). 26,27 Therefore, the strength of the interactions of these proteins with a negatively charged TMA coated surface would be different, which can lead to different adsorption patterns on a TMA modified surface. The adsorption behavior of BSA and lysozyme was studied in a wide pH range in addition to the measurement of the surface potential during the protein interaction.…”