This thesis focuses on the development of NMR methods suitable for the measurement of scalar and dipolar couplings in biological macromolecules, particularly in proteins. In section 4, based on study I, a method designed for the measurement of the structurally important 3JHNHα coupling constant is described. In section 5, based on studies II-IV, the focus shifts to methods suitable for the measurement of several dipolar couplings observable in anisotropic media. The goal has been to develop pulse sequences appropriate for measuring coupling constants with reasonable accuracy, convenience, and sensitivity. Most of the pulse sequences described in this thesis are modifications of those pulse sequences presented in original papers I-IV. For instance, many pulse sequences are revised to take advantage of gradient selection and inclusion of 15N steady-state magnetization, in order to improve artefact suppression and overall sensitivity.