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

作者：Soares T; Christen M; Hu KF; van Gunsteren WF^*

来源：Tetrahedron, 2004, 60(35): 7775-7780.

DOI：10.1016/j.tet.2004.06.062

• alpha-peptide
• beta-peptide
• molecular dynamics simulation
• peptide folding
• conformation analysis

beta-Polypeptides are known to adopt helical secondary structure in organic solvents, even for rather short chain lengths. It is investigated whether a short alpha-polypeptide with amino-acid side chains that enable beta-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 beta-peptides regarding helix stability.

• 出版日期2004-8-23