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 journalArticle

1 Citation (Scopus)

Abstract

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
Volume39
Issue number2
DOIs
Publication statusPublished - 2018 Feb 1

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Hydrogen bonds
Peptides
Nuclear magnetic resonance
Depsipeptides
X rays

All Science Journal Classification (ASJC) codes

  • Chemistry(all)

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Jang, Geunhyuk ; Lee, Mihye ; Lee, Jaeyeon ; Shim, Jihyun ; Kang, Philjae ; Choi, Moon Gun ; Choi, Soo Hyuk. / Cooperative Effect of the Two Hydrogen Bonding Types on 11/9-Helical Folding of α/β-Peptides. In: Bulletin of the Korean Chemical Society. 2018 ; Vol. 39, No. 2. pp. 244-249.
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Cooperative Effect of the Two Hydrogen Bonding Types on 11/9-Helical Folding of α/β-Peptides. / Jang, Geunhyuk; Lee, Mihye; Lee, Jaeyeon; Shim, Jihyun; Kang, Philjae; Choi, Moon Gun; Choi, Soo Hyuk.

In: Bulletin of the Korean Chemical Society, Vol. 39, No. 2, 01.02.2018, p. 244-249.

Research output: Contribution to journalArticle

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