We have recently developed and implemented two experiments in biomolecular NMR for an undergraduate-level biophysical chemistry laboratory with commercially available [subscript 15]N-enriched human ubiquitin. These experiments take advantage of [subscript 15]N direct detection of the NMR signal. The first experiment develops skills in acquiring and interpreting one-dimensional and two-dimensional NMR data of an aqueous protein sample (D. Rovnyak, L. E. Thompson (2005) "An accessible two-dimensional solution nuclear magnetic resonance experiment on human ubiquitin," "Biochem. Mol. Biol. Educ." 33, 117-122). In the second experiment, discussed here, students examine the overall dynamics of a protein in solution. Students measure spin relaxation times T[subscript 1] and T[subscript 2] and use these data to estimate a rotational correlation time, tau[subscript c], and the diameter of ubiquitin using the Stokes-Einstein relation. This is a fast and simple experiment, requiring about 1 h of instrument time, and a valuable opportunity to provide a hands-on experience in studying macromolecular size and dynamics. This experiment is conducted in synchrony with lecture material on hydrodynamics and sedimentation.