title: Analyzing protein-ligand interactions by dynamic NMR spectroscopy.
abstract: Nuclear magnetic resonance (NMR) spectroscopy can provide detailed information on protein-ligand interactions that is inaccessible using other biophysical techniques. This chapter focuses on NMR-based approaches for extracting affinity and rate constants for weakly binding transient protein complexes with lifetimes of less than about a second. Several pulse sequences and analytical techniques are discussed, including line-shape simulations, spin-echo relaxation dispersion methods (CPMG), and magnetization exchange (EXSY) experiments.
authors.affiliation: Department of Chemistry, McGill University, Montreal, QC, Canada.
authors.forename: Anthony
authors.initials: A
authors.lastname: Mittermaier
authors.forename: Erick
authors.initials: E
authors.lastname: Meneses
mesh_terms: D007700:Kinetics; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy / Q000295:instrumentation / Q000379:methods*; D010455:Peptides / Q000737:chemistry*; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D008024:Ligands; D010455:Peptides; D011506:Proteins