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Structural Characterization of α/β‐Peptides having Alternating Residues: X‐ray Structures of the 11/9‐Helix from Crystals of Racemic Mixtures

2013; Wiley; Volume: 52; Issue: 48 Linguagem: Inglês

10.1002/anie.201306404

1521-3773

Mihye Lee, Jihyun Shim, Philjae Kang, Ilia A. Guzei, Soo Hyuk Choi,

RNA and protein synthesis mechanisms

Twisted (crystal)sisters: The structures of the α/β-peptide 11/9-helix were determined by single-crystal X-ray crystallography. The racemic compounds adopt centrosymmetric crystal packing, and display fully folded 11/9-helical conformations. The helical parameters of the 11/9-helix are analogous to those of the 310-helix, despite different hydrogen-bonding types. As a service to our authors and readers, this journal provides supporting information supplied by the authors. Such materials are peer reviewed and may be re-organized for online delivery, but are not copy-edited or typeset. Technical support issues arising from supporting information (other than missing files) should be addressed to the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.