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- W3075399533 abstract "Abstract The effect of glycine, L-alanine, DL-α-aminobutyric acid, in combination with each other and with a sugar alcohol sorbitol has been examined on the globular protein hen egg-white lysozyme. The objective of the work is to examine if synergy operates in these systems and to understand if sorbitol which has several hydroxyl groups can alter the effect of osmolytes on protein. A combination of uv-visible, fluorescence, circular dichroism spectroscopies, and high sensitivity isothermal titration calorimetry have been employed to address the changes in thermal stability and conformation of the protein in the presence of mixture of these osmolytes. The values of heats of interaction of the protein with mixture of osmolytes and those of interaction of one osmolyte with the other have been determined in arriving at the proposed mode of action. Thermodynamic signatures of interaction between the osmolytes have been correlated with transition temperature and conformation of the protein to unravel the mode of action in defining extent or occurrence of synergy in these systems. Further, the results have been interpreted to obtain experimental evidence for the proposed mode of action which suggests absence of appreciable interaction among these osmolytes in mixture and occurrence of individual action in preferential hydration of the protein." @default.
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- W3075399533 date "2020-11-01" @default.
- W3075399533 modified "2023-10-16" @default.
- W3075399533 title "Unraveling thermodynamic and conformational correlations in action of osmolytes on hen egg white lysozyme" @default.
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- W3075399533 doi "https://doi.org/10.1016/j.molliq.2020.113996" @default.
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