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Zeitschrift für Kristallographie - Crystalline Materials

Editor-in-Chief: Pöttgen, Rainer

Ed. by Antipov, Evgeny / Boldyreva, Elena V. / Friese, Karen / Huppertz, Hubert / Jahn, Sandro / Tiekink, E. R. T.

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Volume 212, Issue 11


Unusual conformations adopted by standard amino acids in Aib-containing oligopeptides

R. Geßmann / M. Kokkinidis / M. Currle / H. Brückner
Published Online: 2010-07-28 | DOI: https://doi.org/10.1524/zkri.1997.212.11.819


The structures of the protected tetrapeptides Z-Aib-Aib-Aib-Val-OtBu (I) and Z-Val-Aib-Aib-Gln-OtBu (II), which contain the conformationally constrained residue α-aminoisobutyric acid (Aib), have been studied by X-ray crystallography. Both molecules in the asymmetric unit of I adopt left-handed 310-helical conformation, stabilized both by two 4 → 1 intramolecular hydrogen bonds. The structure of II consists of a β-turn of type II and a consecutive β-turn of type III′ and is extended at the C-terminus. This structure is stabilized by three intramolecular hydrogen bonds. All non-Aib residues (Val, Gln) in I and II adopt rather unusual backbone conformations compared with other helical structures in proteins.

About the article

Published Online: 2010-07-28

Published in Print: 1997-11-01

Citation Information: Zeitschrift für Kristallographie - Crystalline Materials, Volume 212, Issue 11, Pages 819–825, ISSN (Online) 2196-7105, ISSN (Print) 2194-4946, DOI: https://doi.org/10.1524/zkri.1997.212.11.819.

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