Measurement of homonuclear three-bond J(H(N)Halpha) coupling constants in unlabeled peptides complexed with labeled proteins: application to a decapeptide inhibitor bound to the proteinase domain of the NS3 protein of hepatitis C virus (HCV)

J Biomol NMR. 2001 May;20(1):23-9. doi: 10.1023/a:1011281527761.

Abstract

A new isotope-filtered experiment has been designed to measure homonuclear three-bond J(H(N)Halpha) coupling constants of unlabeled peptides complexed with labeled proteins. The new experiment is based on the 3D HNHA pulse scheme, and belongs to the 'quantitative J-correlation' type. It has been applied to a decapeptide inhibitor bound to the proteinase domain of the NS3 protein of human hepatitis C virus (HCV).

MeSH terms

  • Algorithms*
  • Antiviral Agents / chemistry*
  • Antiviral Agents / metabolism
  • Hepacivirus / chemistry
  • Hepacivirus / drug effects*
  • Macromolecular Substances
  • Nuclear Magnetic Resonance, Biomolecular*
  • Oligopeptides / chemistry*
  • Oligopeptides / metabolism
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism
  • Protease Inhibitors / chemistry*
  • Protease Inhibitors / metabolism
  • Protein Structure, Tertiary
  • Viral Nonstructural Proteins / chemistry*
  • Viral Nonstructural Proteins / metabolism

Substances

  • Antiviral Agents
  • Macromolecular Substances
  • NS3 protein, hepatitis C virus
  • Oligopeptides
  • P775 protein, synthetic
  • Peptide Fragments
  • Protease Inhibitors
  • Viral Nonstructural Proteins