Membrane proteins are essential for transferring information and materials across cell membranes. The malfunctioning of membrane proteins often has pathological consequences, so such proteins have been primary targets of drug development. Thus, understanding the functional mechanisms of membrane proteins is of great interest in biological, medical, and pharmaceutical fields. Given that the dynamics of membrane proteins is critical for them to exert their functions, the functional mechanisms of membrane proteins cannot be fully described by static snapshots. To this end, NMR is an optimal technique to obtain insights into such dynamics under physiologically relevant conditions. NMR's role has become even more important given the recent advances in the field of membrane protein structural biology driven by X-ray crystallography and cryo-electron microscopy. Here, we describe the recent developments of NMR strategies to analyze the structure and dynamics of multi-spanning membrane proteins, expression and stable-isotope-labeling strategies, reconstruction techniques, and measurement techniques. Although the slow tumbling rates of membrane proteins often pose challenges, there are many representative examples of the application of solution NMR to membrane proteins. Here, we discuss the technical and applicational advances of solution NMR and describe its critical role in further advancing the structural study of membrane proteins.