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S. Ro, C.-J. Yoon
Conformational Preference of Acetyl-Azaalanine-N-Methyl Amide
Conformational preference of Ac-AzAla-NHMe has been investigated using ab initio calculations. Azaalanine in peptides prefer to adopt two conformational families including four conformations in which (φ,ψ) are (-90°, -13°), (90°, 13°), (-70°, 164°) and (70°, -164°). The stability at φ = &plusm;90° is explained by repulsion of lone pairs on the nitrogens and hydrogen bonding between Ac-N and terminal N(Me)H. On the other hand, the angle ψ adopts only ~0° or 180° since the N(Me)-C(O) bond has double bond character. One conformational family in which the (φ,ψ) torsion angles are (-90°, -13°) or (90°, 13°), is similar to the i+2 position of typical β-I or β-II turns. The other conformation in which the (φ,ψ) torsion angles are (-70°, 164°) or (70°, -164°), is similar to the polyproline II structure appearing in collagen. We believe that these results are useful in designing constrained peptidomimetics for drug discovery and peptide engineering.
Zeitschrift für Physikalische Chemie, Oldenbourg Wissenschaftsverlag
Print ISSN: 0942-9352
Volume: 214, 12/2000
Pages: 1699