1. Crystal structure ofN-(tert-butoxycarbonyl)glycyl-(Z)-β-bromodehydroalanine methyl ester [Boc–Gly–(β-Br)(Z)ΔAla–OMe]
- Author
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Krzysztof Ejsmont, Maciej Makowski, Bartosz Zarychta, and Paweł Lenartowicz
- Subjects
inorganic chemicals ,crystal structure ,Stereochemistry ,education ,Crystal structure ,behavioral disciplines and activities ,Research Communications ,Steric repulsion ,lcsh:Chemistry ,chemistry.chemical_compound ,dehydroamino acid ,β-bromodehydroalanine ,dehydroamino acid ,non-helical conformation ,General Materials Science ,[beta]-bromodehydroalanine ,Amino acid residue ,health care economics and organizations ,Quantitative Biology::Biomolecules ,Dipeptide ,Chemistry ,Hydrogen bond ,General Chemistry ,hydrogen bonding ,Condensed Matter Physics ,humanities ,lcsh:QD1-999 ,β-bromodehydroalanine ,Alanine methyl ester - Abstract
In a dehydroamino acid with a C=C bond between the α- and β-C atoms, the amino acid residues are linked trans to each other and there are no strong intramolecular hydrogen bonds. The torsion angles indicate a non-helical conformation of the molecule., The title compound, C11H17BrN2O5, is a dehydroamino acid with a C=C bond between the α- and β-C atoms. The amino acid residues are linked trans to each other and there are no strong intramolecular hydrogen bonds. The torsion angles indicate a non-helical conformation of the molecule. The dipeptide folding is influenced by an intermolecular N—H⋯O hydrogen bond and also minimizes steric repulsion. In the crystal, molecules are linked by strong N—H⋯O hydrogen bonds, generating (001) sheets. The sheets are linked by weak C—H⋯O and C—H⋯Br bonds and short Br⋯Br [3.4149 (3) Å] interactions.
- Published
- 2014