title: Transverse relaxation optimised spin-state selective NMR experiments for measurement of residual dipolar couplings.
abstract: Three transverse relaxation optimised NMR experiments (TROSY) for the measurement of scalar and dipolar couplings suitable for proteins dissolved in aqueous iso- and anisotropic solutions are described. The triple-spin-state-selective experiments yield couplings between 1HN-13Calpha, 15N-13Calpha, 1HN-13Calpha(i-1), 15N-13Calpha(i-1), 1HN-13C'(i-1), 15N-13C'(i-1) and 13C'(i-1)-13Calpha(i-1) without introducing nonessential spectral crowding compared with an ordinary two-dimensional 15N-1H correlation spectrum and without requiring explicit knowledge of carbon assignments. This set of alpha/beta-J-TROSY experiments is most useful for perdeuterated proteins in studies of structure-activity relationships by NMR to observe, in addition to epitopes for ligands, also conformational changes induced by binding of ligands.
authors.affiliation: Institute of Biotechnology, NMR Laboratory, University of Helsinki, Finland.
authors.forename: P
authors.initials: P
authors.lastname: Permi
authors.forename: A
authors.initials: A
authors.lastname: Annila
mesh_terms: D002247:Carbon Isotopes; D006859:Hydrogen; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D011506:Proteins / Q000737:chemistry*; D012996:Solutions
chemical_list: D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D011506:Proteins; D012996:Solutions; D006859:Hydrogen