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Three complete turns of a 310‐helix at atomic resolution: the crystal structure of Z‐(Aib)11‐OtBu

The crystal structure of the synthetic protected oligopeptide Z‐(Aib)11‐OtBu was determined by x‐ray crystallography. The undecapeptide folds in a regular 310‐helix with nine consecutive 4 → 1 hydrogen bonds. At present, this is the largest available structure of a homopeptide (including homopeptides consisting of standard amino acids) and also the longest observed regular 310‐helix at atomic resolution. Z‐(Aib)11‐OtBu crystallizes readily from hot ethanol–water mixture and is one of the crystals in which no solvent molecule is co‐crystallized. In the crystal head‐to‐tail hydrogen bonded columns are formed in the [1 0 1] direction. Each helical column is surrounded by six others, whereby two are packed in parallel and four in antiparallel fashion. Helical columns are packed via apolar crystal contacts. The crystal structure of Z‐(Aib)11‐OtBu is compared with the crystal structures of Z‐(Aib)10‐OtBu and Z‐(Aib)9‐OtBu. The similarities and differences are analysed. Copyright © 2003 European Peptide Society and John Wiley & Sons, Ltd.