Trapping a folding intermediate of the alpha-helix: stabilization of the pi-helix. Academic Article uri icon

Overview

abstract

  • We report the design, synthesis, and characterization of a short peptide trapped in a pi-helix configuration. This high-energy conformation was nucleated by a preorganized pi-turn, which was obtained by replacing an N-terminal intramolecular main chain i and i + 5 hydrogen bond with a carbon-carbon bond. Our studies highlight the nucleation parameter as a key factor contributing to the relative instability of the pi-helix and allow us to estimate fundamental helix-coil transition parameters for this conformation.

publication date

  • March 13, 2008

Research

keywords

  • Peptides
  • Protein Folding

Identity

PubMed Central ID

  • PMC7183248

Scopus Document Identifier

  • 41849126420

Digital Object Identifier (DOI)

  • 10.1021/bi800136m

PubMed ID

  • 18335996

Additional Document Info

volume

  • 47

issue

  • 14