Structural characterization of α/β-peptides having alternating residues: X-ray structures of the 11/9-helix from crystals of racemic mixtures

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

Research output: Contribution to journalArticle

32 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)12564-12567
Number of pages4
JournalAngewandte Chemie - International Edition
Volume52
Issue number48
DOIs
Publication statusPublished - 2013 Nov 25

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Peptides
X rays
Crystals
X ray crystallography
Conformations
Hydrogen bonds
Single crystals

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)

Cite this

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

In: Angewandte Chemie - International Edition, Vol. 52, No. 48, 25.11.2013, p. 12564-12567.

Research output: Contribution to journalArticle

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