[en] 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 ¹H^N-¹³C^α, ¹⁵N-¹³C^α, ¹H^N-¹³C^α_i-1, ¹⁵N-¹³C^α_i-1, ¹H^N-¹³C'_i-1, ¹⁵N-¹³C'_i-1, and ¹³C'_i-1-¹³C^α_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 α/β-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