Title : Thermodynamic analysis of ANS binding to partially unfolded α-lactalbumin: correlation of endothermic to exothermic changeover with formation of authentic molten globules.

Pub. Date : 2016 Sep

PMID : 27060481






2 Functional Relationships(s)
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1 We expect that the thermodynamic properties obtained from this study would serve as a useful reference for investigating the binding of other hydrophobic ligands such as oleic acid to apo-BLA, because oleic acid is known to have tumor-selective cytotoxicity when complexed with partially unfolded alpha-lactalbumin. Oleic Acid lactalbumin alpha Bos taurus
2 We expect that the thermodynamic properties obtained from this study would serve as a useful reference for investigating the binding of other hydrophobic ligands such as oleic acid to apo-BLA, because oleic acid is known to have tumor-selective cytotoxicity when complexed with partially unfolded alpha-lactalbumin. Oleic Acid lactalbumin alpha Bos taurus