Abstract

Phase transformations of bovine serum albumin (BSA) are investigated using the Brilluoin light scattering in the temperature range from 300 to 380 K in solutions with concentrations of 50 and 5 mg/mL. As the reference sequence, the sequence of phase transformations in a concentrated (100 mg/mL) BSA solution are used for analyzing the results. It is shown that the sequence of BSA phase transformations is modified upon a decrease in the concentration. For example, in the vicinity of denaturation, the region with fibrilform protein aggregates disappears, and the properties of gel-type high-temperature phase change.

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