Nuclear magnetic resonance (NMR) spectroscopy, isothermal titration calorimetry (ITC), and differential scanning calorimetry (DSC) provide different, yet highly complementary views of biomolecular dynamics and energetics. NMR quantifies internal motions over a wide range of time scales with atomic resolution. Calorimetry is extremely sensitive to the energetics of conformational transitions and macromolecular interactions. Together, they can yield detailed, quantitative descriptions of biomolecular function that are inaccessible to any of the techniques alone. This Chapter outlines the ITC, DSC and several NMR dynamics methodologies, and gives an overview of selected applications that highlight the potential of combining NMR and calorimetry.