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• W2024973824 abstract "The secondary structure of bovine serum albumin (BSA) was first examined in the thermal denaturation up to 130 °C. The helicity (66%) of the protein decreased with rise of temperature. Half of the original helicity was lost at 80 °C, but the helicity of 16% was still maintained even at 130 °C. When the BSA solution was cooled down to 25 °C after heating at temperatures above 50 °C, the helicity was not completely recovered. The higher the thermal denaturation temperature was, the lower was the recovered helicity. On the other hand, upon the addition of sodium dodecyl sulfate (SDS), the secondary structure of BSA was partially protected against the thermal denaturation above 50 °C where the structural change became irreversible. A particular protective effect was observed below 85 °C upon the coexistence of SDS of extremely low concentrations. For example, the helicity was 34% at 80 °C in the absence of SDS, but it was maintained at 58% at the same temperature upon the coexistence of 0.75 mM SDS. Upon cooling down from 80 to 25 °C, the helicity of BSA was recovered to 62% in the presence of 0.75 mM SDS. Such a protective effect of SDS was not observed above 95 °C. In the interaction with the surfactant, this protein structure appeared likely to have a critical temperature between 90 and 100 °C in addition to the critical temperature in the vicinity of 50 °C. This protective effect of SDS, characterized by the specific amphiphilic nature of this anionic surfactant, is considered to be attained by building cross-linking bridges between particular nonpolar residues and particular positively charged residues in the protein molecule." @default.
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• W2024973824 date "2008-12-02" @default.
• W2024973824 modified "2023-10-18" @default.
• W2024973824 title "Secondary Structural Change of Bovine Serum Albumin in Thermal Denaturation up to 130 °C and Protective Effect of Sodium Dodecyl Sulfate on the Change" @default.
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• W2024973824 doi "https://doi.org/10.1021/jp8067624" @default.
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