Stabilization of α-helix structure by polar side-chain interactions: Complex salt bridges, cation-π interactions, and C-H···O H-bonds

Zhengshuang Shi, C. Anders Olson, Anthony J. Bell, Neville R. Kallenbach

Research output: Contribution to journalReview article

Abstract

It is generally understood that helical proteins are stabilized by a combination of hydrophobic and packing interactions, together with H-bonds and electrostatic interactions. Here we show that polar side-chain interactions on the surface can play an important role in helix formation and stability. We review studies on model helical peptides that reveal the effect of weak interactions between side chains on helix stability, focusing on some nonclassical side-chain-side-chain interactions: complex salt bridges, cation-π, and C-H···O H-bonding interactions. Each of these can be shown to contribute to helix stability, and thus must be included in a comprehensive catalogue of helix stabilizing effects. The issue of the structure of the unfolded states of helical peptides is also discussed, in the light of recent experiments showing that these contain substantial amounts of polyproline II conformation.

Original languageEnglish (US)
Pages (from-to)366-380
Number of pages15
JournalBiopolymers - Peptide Science Section
Volume60
Issue number5
DOIs
StatePublished - Jan 1 2001

Keywords

  • C-H···O H-bonding interactions
  • Cation-π interactions
  • Complex salt bridge interactions
  • Helical proteins
  • Polar side-chain interactions

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Biomaterials
  • Organic Chemistry

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