Study of Desiccation-Induced Structural Changes of G3LEA Peptides Using Replica Exchange Molecular Dynamics Simulation

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  • レプリカ交換分子動力学法を用いたLEAペプチドの乾燥誘導構造変化 の解析
  • レプリカ コウカン ブンシ ドウリキガクホウ オ モチイタ LEA ペプチド ノ カンソウ ユウドウ コウゾウ ヘンカ ノ カイセキ

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Abstract

Group-3 late embryogenesis abundant (G3LEA) proteins are expressed in anhydrobiotic organisms experiencing desiccation stress and their major segments consist of repeats of weakly conserved 11-mer amino acid motifs. It is known that the 11-mer motifs are disordered in aqueous solution but form -helical coiled coil structure in dry state. However, little information has been obtained with regard to the underlying mechanism of such structural change. Here, we performed replica exchange molecular dynamics (REMD) simulations for a short model peptide, called PvLEA-22, in which the 11-mer motif is repeated two times. In addition, for comparison similar simulations were performed for a scrambled peptide without such sequence regularity. The simulation successfully reproduced that the content of -helix of the PvLEA-22 increases with a decrease in water content, while the major structure of the scrambled peptide remained disordered even in the dry state. On the basis of these results, we discuss the structural change mechanism of PvLEA-22.

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