There are 826 G protein-coupled receptors (GPCR) in the human proteome, which regulate key physiological processes and have therefore long been attractive as drug targets. With crystal structure determinations of more than 50 different human GPCRs during the last decade, an initial platform for structure-based rational design was established for drugs that target GPCRs. The principal method used for our own research is nuclear magnetic resonance (NMR) spectroscopy in solution, which is one of the key approaches for expanding the crystal structure platform with dynamics features of GPCRs at near-physiological conditions. In this context it is of special interest that NMR measurements can be performed without extensive modifications of the GPCRs, such as those used to facilitate crystallization, i.e., by amino acid replacements and/or fusion with other proteins. In my lecture I describe strategies for the use of NMR techniques with GPCRs, which will be illustrated with projects where results obtained with X-ray crystallography or cryo-electron microscopy (cryo-EM) have been complemented with NMR investigations in solution, and discuss the impact of this integrative approach on GPCR biology and drug discovery. References Liu, J.J., Horst, R., Katritch, V., Stevens, R.C. and Wüthrich, K. (2012) Science 335, 1106-1110. Biased signaling pathways in β2-adrenergic receptor characterized by 19F-NMR. Eddy, M., Lee, M.-Y., Gao, Z.-G., White, K.L., Didenko, T., Horst, R., Audet, M., Stanczak, P., McClary, K.M., Han, G.W., Jacobson, K.A., Stevens, R. and Wüthrich, K. (2018) Cell 172, 68–80. Allosteric coupling of drug binding and intracellular signaling in the A2A adenosine receptor.