Cooperative Effect of the Two Hydrogen Bonding Types on 11/9-Helical Folding of α/β-Peptides

Geunhyuk Jang, Mihye Lee, Jaeyeon Lee, Jihyun Shim, Philjae Kang, Moon Gun Choi, Soo Hyuk Choi

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)


α/β-Peptide 11/9-helix is an unconventional helical structure in which 11- and 9-membered ring hydrogen bonds alternate along the helical axis. We have examined the interplay and the relative strength of these two hydrogen bonding types by IR, NMR, and X-ray crystallographic methods. A pair of two adjacent hydrogen bonds with opposite directionality cooperatively stabilized each other in non-hydrogen-bonding solvents. In contrast, an unpaired hydrogen bond was unstable to promote helical folding. The IR and the NMR data of α/β-depsipeptides suggested that a 9-membered ring hydrogen bond is favored over an 11-membered ring hydrogen bond.

Original languageEnglish
Pages (from-to)244-249
Number of pages6
JournalBulletin of the Korean Chemical Society
Issue number2
Publication statusPublished - 2018 Feb

Bibliographical note

Publisher Copyright:
© 2018 Korean Chemical Society, Seoul & Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim

All Science Journal Classification (ASJC) codes

  • Chemistry(all)


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