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
Link To Document :
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