Neighbor effect on PPII conformation in alanine peptides

Kang Chen, Zhigang Liu, Chunhui Zhou, Zhengshuang Shi, Neville R. Kallenbach

Research output: Contribution to journalArticle

Abstract

The polyproline II (PPII) conformation is dominant in short alanine oligomers. The noncooperativity of PPII structure in alanine peptides indicates that PPII in water is locally determined and that alanine neighbors are consistent with Flory's isolated pair hypothesis. However, neighbor effects from β-branched or bulky aromatic residues tend to increase the Φ angle of the nearest neighbor as observed in coil library data. Here we demonstrate directly the neighbor effect using short alanine model peptides GGAAAGG, GGLnALnGG (Ln is norleucine), GGIAAGG, and GGIAIGG. The far-UV CD spectra, NMR 3JαN coupling constant, and H-D hydrogen exchange measurements reveal that Ile reduces the PPII content of the probe Ala side chain relative to Ala or norLeu. The free energy differences are consistent with predictions from electrostatic solvation free energy (ESF) calculations. The results indicate that prediction of PPII propensities or scales requires including the neighbor effect.

Original languageEnglish (US)
Pages (from-to)10146-10147
Number of pages2
JournalJournal of the American Chemical Society
Volume127
Issue number29
DOIs
StatePublished - Jul 27 2005

ASJC Scopus subject areas

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

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    Chen, K., Liu, Z., Zhou, C., Shi, Z., & Kallenbach, N. R. (2005). Neighbor effect on PPII conformation in alanine peptides. Journal of the American Chemical Society, 127(29), 10146-10147. https://doi.org/10.1021/ja052094o