The structural analysis of membrane proteins is one of the major challenges in biophysical chemistry today. This arises because these proteins prefer an environment that is neither crystal nor solution. Unfortunately, crystal and solution phases are the only two phases for which structure determination methods are well established. We have undertaken the development of NMR based structure determination methods that are applicable in a medium that mimics the partial, liquid crystalline order natural membranes. These methods are currently being applied to peptides that present typical membrane protein structural motifs, such as trans bilayer helices and surface associated amphipathic helices.