Crystallographic characterization of the α/β-peptide 14/15-helix

Soo Hyuk Choi, Ilia A. Guzei, Samuel H. Gellman

Research output: Contribution to journalArticle

49 Citations (Scopus)

Abstract

We report the first high-resolution structural data for the 14/15-helix, a secondary structure that is formed by oligomers with a 1:1 alternation of α- and β-amino acid residues. Previously, we concluded from NMR data that short α/β-peptides containing cyclopentane-constrained β-residues display rapid interconversion between two helical folding patterns, the 11-helix (i,i+3 C=O⋯H-N H-bonds) and the 14/15-helix (i,i+4 C=O⋯H-N H-bonds). Subsequent work in other laboratories, however, has called this hypothesis into question. Partial support for our original hypothesis was obtained when we obtained the first crystal structure in this α/β-peptide series, which revealed an 11-helical conformation. The present report of a 14/15-helical conformation strengthens the original hypothesis.

Original languageEnglish
Pages (from-to)13780-13781
Number of pages2
JournalJournal of the American Chemical Society
Volume129
Issue number45
DOIs
Publication statusPublished - 2007 Nov 14

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Peptides
Conformations
Cyclopentanes
Oligomers
Amino acids
Crystal structure
Nuclear magnetic resonance
Amino Acids
hydroxide ion

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

Choi, Soo Hyuk ; Guzei, Ilia A. ; Gellman, Samuel H. / Crystallographic characterization of the α/β-peptide 14/15-helix. In: Journal of the American Chemical Society. 2007 ; Vol. 129, No. 45. pp. 13780-13781.
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Crystallographic characterization of the α/β-peptide 14/15-helix. / Choi, Soo Hyuk; Guzei, Ilia A.; Gellman, Samuel H.

In: Journal of the American Chemical Society, Vol. 129, No. 45, 14.11.2007, p. 13780-13781.

Research output: Contribution to journalArticle

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AB - We report the first high-resolution structural data for the 14/15-helix, a secondary structure that is formed by oligomers with a 1:1 alternation of α- and β-amino acid residues. Previously, we concluded from NMR data that short α/β-peptides containing cyclopentane-constrained β-residues display rapid interconversion between two helical folding patterns, the 11-helix (i,i+3 C=O⋯H-N H-bonds) and the 14/15-helix (i,i+4 C=O⋯H-N H-bonds). Subsequent work in other laboratories, however, has called this hypothesis into question. Partial support for our original hypothesis was obtained when we obtained the first crystal structure in this α/β-peptide series, which revealed an 11-helical conformation. The present report of a 14/15-helical conformation strengthens the original hypothesis.

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