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The crystal structure of Z‐Gly‐Aib‐Gly‐Aib‐OtBu
Author(s) -
Gessmann Renate,
Brückner Hans,
Aivaliotis Michalis,
Petratos Kyriacos
Publication year - 2015
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.2764
Subject(s) - chemistry , molecule , hydrogen bond , crystal structure , crystallography , residue (chemistry) , peptide , crystal (programming language) , stereochemistry , ether , organic chemistry , biochemistry , computer science , programming language
The synthetic peptide Z‐Gly‐Aib‐Gly‐Aib‐OtBu was dissolved in methanol and crystallized in a mixture of ethyl acetate and petroleum ether. The crystals belong to the centrosymmetric space group P 4/ n that is observed less than 0.3% in the Cambridge Structural Database. The first Gly residue assumes a semi‐extended conformation ( φ ±62°, ψ ∓131°). The right‐handed peptide folds in two consecutive β ‐turns of type II' and type I or an incipient 3 10 ‐helix, and the left‐handed counterpart folds accordingly in the opposite configuration. In the crystal lattice, one molecule is linked to four neighbors in the ab ‐plane via hydrogen bonds. These bonds form a continuous network of left‐ and right‐handed molecules. The successive ab ‐planes stack via apolar contacts in the c ‐direction. An ethyl acetate molecule is situated on and close to the fourfold axis. Copyright © 2015 European Peptide Society and John Wiley & Sons, Ltd.