Nuclear magnetic resonance (NMR) spectroscopy provides information regarding the structure and dynamics for protein, RNA and DNA at the atomic level. These biomolecules may be studied individually or in the presence of ligands or other biomolecules. Determination of the three-dimensional structure of macromolecules and their complexes is vital for rational drug design and expanding knowledge within the field of mechanistic biology. The term “biomolecular NMR” refers to the use of NMR to study biological compounds in vivo or under conditions which best mimic in vivo conditions. Although most cytosolic proteins are relatively easy to study, membrane proteins require lipophilic environments for stability and function and thus are typically studied in micelles, lipid bilayers, cellular membranes and living cells. NMR generally lacks the sensitivity to detect useful signals from unlabeled sample, therefore biomolecules are often required to be enriched in 13C and/or 15N for analyses. Deuterium is often incorporated to simplify spectra or to alter relaxation effects so that the necessary spectroscopic information may be acquired. Over the years, advances in isotope-labeling strategies have expanded the size of macromolecules and the types of detailed information available for study.