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「Biophysics and Physicobiology」にTatsushi Nishimoto et al. “Replica exchange molecular dynamics simulation study on the mechanism of desiccation-induced structuralization of an intrinsically disordered peptide as a model of LEA proteins”を掲載

2019年11月29日 学会から

日本生物物理学会欧文誌[Biophysics and Physicobiology]に以下の論文が新規掲載されました。

Tatsushi Nishimoto, Yuta Takahashi, Shohei Miyama, Tadaomi Furuta, Minoru Sakurai “Replica exchange molecular dynamics simulation study on the mechanism of desiccation-induced structuralization of an intrinsically disordered peptide as a model of LEA proteins”

【Significance】
Intrinsically disordered property of group 3 late embryogenesis abundant peptide

Group 3 late embryogenesis abundant (G3LEA) proteins are disordered in solution, but they structuralize into an α-helical structure during drying. To elucidate the origin of this unusual property, we performed replica exchange MD simulations for a peptide composed of two tandem repeat of an 11-mer motif characteristic to G3LEA proteins. It was revealed that its single chain alone exhibits no structuralization, but its two-helix bundle forms a left-handed α-helical coiled coil in the dry state. These results support the cytoskeleton hypothesis that has been proposed as a mechanism by which G3LEA proteins work as a desiccation protectant in anhydrobiotic organisms.

Biophysics and Physicobiology, Vol.16, 196-204
URL: https://doi.org/10.2142/biophysico.16.0_196


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