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

Honami Sakaizawa, Hiroshi C. Watanabe, Tadaomi Furuta, Minoru Sakurai

研究成果: Article査読

3 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)114-118
ページ数5
ジャーナルChemical Physics Letters
643
DOI
出版ステータスPublished - 2016 1月

ASJC Scopus subject areas

  • 物理学および天文学(全般)
  • 物理化学および理論化学

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