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- W2221036651 abstract "Abstract In hydrophilic protein–protein associations, the dehydration penalty, which can cause the formation of a reaction barrier, must be canceled out; however, its mechanism has not been clarified. Here, we explored the possible mechanism through investigation of the dimerization of nucleotide binding domains (NBDs). We assessed the different dimerization processes by molecular dynamics simulations with and without thermal fluctuations in each NBD. Consequently, the reaction barriers of the former and latter were estimated to be ∼100 and ∼15 kcal/mol, respectively, suggesting that thermal fluctuations in the proteins facilitate the exclusion of water molecules from the interfacial region, thereby lowering the barrier." @default.
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- W2221036651 date "2016-01-01" @default.
- W2221036651 modified "2023-10-01" @default.
- W2221036651 title "Thermal fluctuations enable rapid protein–protein associations in aqueous solution by lowering the reaction barrier" @default.
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- W2221036651 doi "https://doi.org/10.1016/j.cplett.2015.11.014" @default.
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