• Title of article

    Alpha- and beta-polypeptides show a different stability of helical secondary structure

  • Author/Authors

    Thereza Soares، نويسنده , , Markus Christen، نويسنده , , Kaifeng Hu، نويسنده , , Wilfred F. van Gunsteren، نويسنده ,

  • Issue Information
    هفته نامه با شماره پیاپی سال 2004
  • Pages
    6
  • From page
    7775
  • To page
    7780
  • Abstract
    β-Polypeptides are known to adopt helical secondary structure in organic solvents, even for rather short chain lengths. It is investigated whether a short α-polypeptide with amino-acid side chains that enable β-peptides to adopt helical structures, can maintain or adopt stable helical structure in methanol or in water. The molecular dynamics simulations do not predict a particular fold, which indicates an essential role for the additional methylene moiety in the backbone of β-peptides regarding helix stability.
  • Keywords
    Alpha-peptide , Beta-peptide , molecular dynamics simulation , Peptide folding , Conformation analysis
  • Journal title
    Tetrahedron
  • Serial Year
    2004
  • Journal title
    Tetrahedron
  • Record number

    1086998