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• W4220809780 abstract "Globular proteins play several essential roles in functioning different mechanisms of the living organisms, and the stability of such protein molecules in an aqueous solution is strongly affected by multivalent ions. In this article, we have systematically studied the effect of temperature (between 5 and 25ºC) on the re-entrant condensation behaviour of bovine serum albumin (BSA) in the presence of trivalent ions, Yttrium (Y3+), and Lanthanum (La3+). The effect of temperature is explained considering the optical properties of the protein, i.e., from the optical absorption and emission behaviours. The absorption in the visible region and the fluorescence emission of BSA becomes maximum at the lowest temperature. The decrement of mobility at lower temperature is responsible for fluorescence enhancement. Moreover, the activation energy of the turbid or viscus phase of the BSA protein under re-entrant condensation is enhanced in comparison with the transparent phase and the corresponding energy value is estimated from the fluorescence study." @default.
• W4220809780 created "2022-04-03" @default.
• W4220809780 creator A5009501890 @default.
• W4220809780 creator A5087048000 @default.
• W4220809780 date "2022-01-29" @default.
• W4220809780 modified "2023-09-26" @default.
• W4220809780 title "Effect of Temperature on Re-entrant Condensation of Globular Protein in Presence of Tri-valent Ions" @default.
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• W4220809780 doi "https://doi.org/10.1007/s10895-021-02874-2" @default.
• W4220809780 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/35091910" @default.
• W4220809780 hasPublicationYear "2022" @default.
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