Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5417356 | Journal of Molecular Structure: THEOCHEM | 2009 | 6 Pages |
Abstract
A complete overview on all possible helix types with unidirectional hydrogen bonds in oligomers of ε-amino acids is given on the basis of a systematical conformational analysis employing ab initio MO theory (HF/6-31Gâ, B3LYP/6-31Gâ, PCM//HF/6-31Gâ). The conformational search provides a wide variety of folding patterns which makes the class of ε-peptides interesting for a rational peptide design by selection of suited backbone substituent patterns. The relationships between the predicted secondary structures for the ε-peptides and other peptide foldamer classes, as for instance α/β-hybrid peptides, are demonstrated.
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Authors
Peter Schramm, Hans-Jörg Hofmann,