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- W2997805286 abstract "Abstract In this work, the combined influence of urea and KI on protein native structure is quantitatively investigated through the comparative molecular dynamics simulations on the structural dynamics of a polypeptide of TRPZIP4 in a series of urea/KI mixed solutions (urea concentration: 4M, KI salt concentration: 0M-6M). The observed enhanced denaturing ability of urea/KI mixture can be explained by direct interactions of urea/K + /water towards protein (electrostatic and vdW interactions from urea and electrostatic interactions from K + and water) and indirect influence of KI on the strengthened interaction of urea towards protein backbone and side-chain. The latter indirect influence is fulfilled through the weakening of hydrogen bonding network among urea and water by the appearance of K + –water and I — urea interactions. As a result, the denaturing ability enhancement of urea and KI mixed solution is induced by the collaborative behavior of urea and KI salt." @default.
- W2997805286 created "2020-01-10" @default.
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- W2997805286 date "2019-12-30" @default.
- W2997805286 modified "2023-09-25" @default.
- W2997805286 title "Collaborative Behavior of Urea and KI in Denaturing Protein Native Structure" @default.
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- W2997805286 doi "https://doi.org/10.1101/2019.12.29.888271" @default.
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