Nuclear magnetic resonance methods for studying protein-ligand complexes

Methods Enzymol. 1994:239:717-39. doi: 10.1016/s0076-6879(94)39027-4.
No abstract available

Publication types

  • Review

MeSH terms

  • Amino Acid Isomerases / chemistry
  • Amino Acid Isomerases / metabolism
  • Animals
  • Binding Sites
  • Carbon Isotopes
  • Carrier Proteins / chemistry
  • Carrier Proteins / metabolism
  • Cyclosporine / chemistry
  • Cyclosporine / metabolism
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / metabolism
  • Deuterium
  • Heat-Shock Proteins / chemistry
  • Heat-Shock Proteins / metabolism
  • Hydrogen
  • Ligands
  • Macromolecular Substances
  • Magnetic Resonance Spectroscopy / methods*
  • Models, Molecular
  • Molecular Probes
  • Molecular Structure
  • Nitrogen Isotopes
  • Peptidylprolyl Isomerase
  • Protein Binding
  • Proteins / chemistry*
  • Proteins / metabolism
  • Tacrolimus / analogs & derivatives
  • Tacrolimus / chemistry
  • Tacrolimus / metabolism
  • Tacrolimus Binding Proteins
  • Thermodynamics

Substances

  • Carbon Isotopes
  • Carrier Proteins
  • DNA-Binding Proteins
  • Heat-Shock Proteins
  • Ligands
  • Macromolecular Substances
  • Molecular Probes
  • Nitrogen Isotopes
  • Proteins
  • Hydrogen
  • Cyclosporine
  • Deuterium
  • immunomycin
  • Amino Acid Isomerases
  • Tacrolimus Binding Proteins
  • Peptidylprolyl Isomerase
  • Tacrolimus