title: Monitoring molecular interactions by NMR.
abstract: The ability of proteins to interact with small molecules or other proteins is essential in all aspects of biology. In many cases these interactions cause detectable changes in NMR chemical shifts, lineshapes, and relaxation rates and therefore provide a means by which to study these biologically important phenomena. Here we review the theory upon which this analysis is based, provide several illustrative examples, and highlight potential problems in the study of binding interactions by solution NMR.
authors.affiliation: Department of Chemistry, Yale University, New Haven, CT, USA.
authors.forename: James M
authors.initials: JM
authors.lastname: Lipchock
authors.forename: J Patrick
authors.initials: JP
authors.lastname: Loria
mesh_terms: D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins