Alpha- and beta-polypeptides show a different stability of helical secondary structure |
| |
Authors: | Thereza Soares |
| |
Institution: | Laboratory of Physical Chemistry, Swiss Federal Institute of Technology Zurich ETH, Hönggerberg, CH-8093 Zürich, Switzerland |
| |
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 |
本文献已被 ScienceDirect 等数据库收录! |
|