The Folding of Trp-cage is Regulated by Stochastic Flip of the Side Chain of Tryptophan

DOI PDF 被引用文献2件 参考文献26件
  • Takunori Yasuda
    College of Biological Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-0821 , Japan
  • Yasuteru Shigeta
    Center for Computational Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-0821 , Japan
  • Ryuhei Harada
    Center for Computational Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-0821 , Japan

抄録

<jats:title>Abstract</jats:title> <jats:p>Trp-cage is an artificial 20-residue protein and forms a hydrophobic core at its central cage upon folding. In the present study, the folding of Trp-cage was addressed by parallel cascade selection molecular dynamics (PaCS-MD). Our results of PaCS-MD indicate that flip of the side chain of tryptophan (W6) was correlated with the overall folding. In conclusion, flip of stochastic side chain of W6 regulates the folding into the native or mis-folded states of Trp-cage.</jats:p>

収録刊行物

  • Chemistry Letters

    Chemistry Letters 50 (1), 162-165, 2020-10-28

    Oxford University Press (OUP)

被引用文献 (2)*注記

もっと見る

参考文献 (26)*注記

もっと見る

関連プロジェクト

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ