2020
DOI: 10.1101/2020.08.26.267799
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Mechanistic Studies of the Stabilization of Insulin Helical Structure by Coomassie Brilliant Blue

Abstract: Human insulin (HI) is an essential protein hormone and its biological activity mostly depends on folded and active conformation in the monomeric state. The present investigation established that Coomassie Brilliant Blue G-250 (CBBG), a small multicyclic hydroxyl compound can reversibly bind to the hormonal protein dimer and maintained most of α-helical folds crucial for biological function of the enzyme. The solution-state 1D NMR and isothermal calorimetric analysis showed a sub-micromolar binding affinity of … Show more

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