Solid-state nuclear magnetic resonance (NMR) spectroscopy has helped provide insights into the organization and investigation of the molecular dynamics of the macromolecular components of cartilage tissue. Here, I provide an overview of solid-state NMR methods and selected application dealing with the structure and dynamics of the glycosaminoglycans and the collagen components of native cartilage tissue, cartilage under osmotic pressure, and cartilage artificially generated using tissue engineering. While the rigid collagen component is detected by cross-polarization NMR techniques either by static or magic-angle spinning NMR, the highly mobile glycosaminoglycans exhibit solution-like behavior and can be studied by high resolution magic-angle spinning NMR methods. Thus, a rather comprehensive picture of the molecular organization and dynamics of the macromolecular components in cartilage emerges, which provides the standard for performing a quality control of tissue-engineered cartilage by NMR spectroscopy.