The tetrapeptide Z-Leu-Aib-Pro-Val-OBg monohydrate

The tetrapeptide Z-Leu-Aib-Pro-Val-OBg monohydrate

The intramolecular hydrogen‐bonding pattern of Z‐Leu‐Aib‐Pro‐Val‐OBg monohydrate [(N‐benzhydryl­amino)­carbonyl­methyl N‐benzyl­oxy­carbonyl‐α‐amino­isobutyryl­prolyl­valinate monohydrate], C43H55N5O8·H2O, is unusual for a tetrapeptide because, in addition to a 14 hydrogen bond, a second hydrogen bo...

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Veröffentlicht in:Acta crystallographica. Section C, Crystal structure communications Crystal structure communications, 2003-08, Vol.59 (8), p.o413-o415
Hauptverfasser: Geßmann, Renate, Schiemann, Norbert, Brückner, Hans, Petratos, Kyriacos
Format: Artikel
Sprache:eng
Schlagworte:
Aminoacids and peptides
Condensed matter: structure, mechanical and thermal properties
Exact sciences and technology
Hydrogen Bonding
Models, Molecular
Oligopeptides - chemistry
Organic compounds
Physics
Protein Conformation
Structure of solids and liquids
crystallography
Structure of specific crystalline solids
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Zusammenfassung:The intramolecular hydrogen‐bonding pattern of Z‐Leu‐Aib‐Pro‐Val‐OBg monohydrate [(N‐benzhydryl­amino)­carbonyl­methyl N‐benzyl­oxy­carbonyl‐α‐amino­isobutyryl­prolyl­valinate monohydrate], C43H55N5O8·H2O, is unusual for a tetrapeptide because, in addition to a 14 hydrogen bond, a second hydrogen bond of the type 15 is formed. This folding reflects the intramolecular hydrogen‐bonding pattern that this amino acid sequence adopts in the naturally occurring peptaibol alamethicin.
ISSN:0108-2701
1600-5759
DOI:10.1107/S0108270103010291