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- W1546096547 abstract "The solubility of amino acids and the preferential solvent interaction of bovine serum albumin in aqueous propylene glycol were investigated by a densimetric method at 25°C. The free energy of most nonpolar side-chains of amino acids decreases and that of the peptide group increases on transferring them from water to aqueous propylene glycol. This shows that propylene glycol molecule could induce weakening of the tertiary structure by hydrophobic bonding and subsequent (or simultaneous) promotion of the helix formation. It was found that at all solvent compositions up to 50% (w/v) propylene glycol (pH 2) this protein preferentially binds the propylene glycol molecule; i.e., the free energy of transfer of the protein to aqueous propylene glycol is negative. The extent increases with increasing propylene glycol contents, in completely parallel fashion with the conformational change or the helix formation of the protein as detected by circular dichroism. The corresponding volume change of transfer of the protein is positive, mainly due to dehydration of the protein accompanying the conformational change. These results demonstrate that the direct protein-solvent interaction is a primary cause of the propylene glycol-induced noncooperative conformational change of proteins." @default.
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- W1546096547 date "1984-05-01" @default.
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- W1546096547 title "The stability of protein structure in aqueous propylene glycol" @default.
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- W1546096547 doi "https://doi.org/10.1016/0167-4838(84)90084-0" @default.
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