Abstract
The small synthetic peptide, benzyl 2-(tert-butoxycarbonyl-amino)isobutyrate, C(16)H(23)NO(4), has the alpha-helical conformation [/varphi/ = 55.8 (2) degrees and /psi/ = 37.9 (2) degrees] observed in peptide fragments of peptaibols containing the alpha-aminoisobutyric acid (Aib) residue. The structure shows no intramolecular hydrogen bonding, which would disrupt the limited conformational freedom associated with this amino acid. Two weak intermolecular hydrogen contacts are observed.
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Schedule a callMore From: Acta crystallographica. Section C, Crystal structure communications
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