The Formation of Hydrophobic Core Regulates the Protein Folding of Villin Elucidated with Parallel Cascade Selection Molecular Dynamics

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Author(s)

Abstract

<p>Villin is a fast-folding protein and has a unique hydrophobic core at the center in its folded form. In the present study, the folding process of Villin was investigated with parallel cascade selection molecular dynamics (PaCS-MD). Our computational results show that formation of the central hydrophobic core was a rate-limiting step in the folding process. In more detail, the folding is regulated with a gathering of four PHE residues to form the hydrophobic core.</p>

Journal

  • Chemistry Letters

    Chemistry Letters 47(10), 1300-1303, 2018

    The Chemical Society of Japan

Codes

  • NII Article ID (NAID)
    130007495956
  • Text Lang
    ENG
  • ISSN
    0366-7022
  • Data Source
    J-STAGE 
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