Volume 57, Issue 4 pp. 487-488

Benzyl tert-but­oxy­carbonyl-α-amino­isobutyrate

Anne-Marie Leduc

Anne-Marie Leduc

Department of Chemistry, University of Louisville, Louisville, KY 40292, USA

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Mark S. Mashuta

Mark S. Mashuta

Department of Chemistry, University of Louisville, Louisville, KY 40292, USA

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Arno F. Spatola

Arno F. Spatola

Department of Chemistry, University of Louisville, Louisville, KY 40292, USA

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First published: 23 June 2004
Mark S. Mashuta, e-mail: [email protected]

Abstract

The small synthetic peptide, benzyl 2-(tert-but­oxy­carbonyl-amino)­isobutyrate, C16H23NO4, has the α-helical conformation [|ϕ| = 55.8 (2)° and |ψ| = 37.9 (2)°] observed in peptide fragments of peptaibols containing the α-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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