Characterization and analysis of binding of Thioflavin T with partially folded and native states of α-lactalbumin protein by calorimetric and spectroscopic techniques

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• 作者：Moumita Dasgupta ; Nand Kishore ; ^{nandk@chem.iitb.ac.in}
• 关键词：α&ndash ; Lactalbumin ; Thioflavin T ; Isothermal titration calorimetry ; Molten globule state ; Binding thermodynamics
• 刊名：International Journal of Biological Macromolecules
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：95
• 期：Complete
• 页码：376-384
• 全文大小：1942 K
• 卷排序：95

文摘

Thioflavin T binding with molten globule and native states of α–lactalbumin studied. Energetics of interactions determined. Fluorescence of Thioflavin T does not increase upon binding molten globule state. Complexation confirmed from calorimetry. Thioflavin T binding can be exploited to characterize intermediate states.