「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 November 29 BPPB
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
