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- W2068135055 abstract "Pressure can retrain the heat-induced aggregation and dissociate the heat-induced aggregates. We observed the aggregation-preventing pressure effect and the aggregates-dissociating pressure effect to characterize the heat-induced aggregation of equine serum albumin (ESA) by FT-IR spectroscopy. The results suggest the α-helical structure collapses at the beginning of heat-induced aggregation through the swollen structure, and then the rearrangement of structure to the intermolecular β-sheet takes place through partially unfolded structure. We determined the activation volume for the heat-induced aggregation (ΔV# = +93 ml/mol) and the partial molar volume difference between native state and heat-induced aggregates (ΔV=+32 ml/mol). This positive partial molar volume difference suggests that the heat-induced aggregates have larger internal voids than the native structure. Moreover, the positive volume change implies that the formation of the intermolecular β-sheet is unfavorable under high pressure." @default.
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- W2068135055 date "2010-03-01" @default.
- W2068135055 modified "2023-10-13" @default.
- W2068135055 title "Pressure effects on the structure, kinetic, and thermodynamic properties of heat-induced aggregation of protein studied by FT-IR spectroscopy" @default.
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- W2068135055 doi "https://doi.org/10.1088/1742-6596/215/1/012156" @default.
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