Thermal fluctuations enable rapid protein-protein associations in aqueous solution by lowering the reaction barrier

Honami Sakaizawa, Hiroshi Watanabe, Tadaomi Furuta, Minoru Sakurai

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1 Citation (Scopus)


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.

Original languageEnglish
Pages (from-to)114-118
Number of pages5
JournalChemical Physics Letters
Publication statusPublished - 2016 Jan 1


ASJC Scopus subject areas

  • Physics and Astronomy(all)
  • Physical and Theoretical Chemistry

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