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

Overview

MeSH

  • Amino Acid Sequence
  • Circular Dichroism
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Structure, Secondary

MeSH Major

  • Peptides
  • Protein Folding

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

  • April 8, 2008

has subject area

  • Amino Acid Sequence
  • Circular Dichroism
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Peptides
  • Protein Folding
  • Protein Structure, Secondary

Research

keywords

  • Journal Article

Identity

Language

  • eng

Digital Object Identifier (DOI)

  • 10.1021/bi800136m

PubMed ID

  • 18335996

Additional Document Info

start page

  • 4189

end page

  • 4195

volume

  • 47

number

  • 14