Publisher Summary This chapter discusses the structural biology of peptides and proteins in synthetic membrane environments by solid-state nuclear magnetic resonance (NMR) spectroscopy. The utility of both orientation and distance constraints has been demonstrated for membrane proteins and polypeptides. The methods have been developed to the point, where illuminating biochemical information has been obtained. There remains considerable work ahead to make the methods more generally applicable through the use of naturally abundant nuclei or uniformly labeled sites. The uniqueness of NMR as a form of spectroscopy is found in the inherent sensitivity of the technique to the nuclear environments. Unlike UV/Vis spectroscopy, which is sensitive to certain infrequent atomic clusters, NMR can be used to study all the atomic sites in a biological macromolecule. Not only is solid state NMR effective for describing the structural detail, high resolution dynamics characterizations are leading to important and novel functional understanding. Through high-resolution structure the details of peptide-solvent interactions will be forthcoming. This too will lead to the functional understanding at a very fundamental biophysical level. Finally, it is important to recognize that this information is being obtained from just the protein systems, for which a new approach for structural elucidation was needed; proteins in an anisotropic environment.