Figure 1. Comparison of micellar, bicellar, and proteoliposomal sample preparations suitable for an NMR‐based study of membrane proteins. In this chapter, MAS‐based studies using proteoliposomal preparations are discussed.

Figure 2. Pictorial representation of schemes of magnetization transfer that can be employed for membrane topology.

Figure 3. Conformational changes of the SRII receptor upon complex formation and light activation as detected by two‐dimensional solid‐state NMR. Residues that are affected (i.e., changes in chemical shift or molecular dynamics) by transducer binding are highlighted on the left SRII structure. Residues highlighted on the right hand SRII structure illustrate areas that underwent chemical shift changes upon light activation.

Figure 4. Graphical summary of solid‐state NMR work on the KcsA–Kv1.3 system. Solid‐state NMR experiments were conducted to study ligand binding, protein dynamics as well as structure and protonation states during different channel states. See main text for further details.

Figure 5. Pictorial representation of the reconstitution of a purified membrane protein. The overexpressed membrane protein carrying the desired affinity tag in the presence of other membrane proteins of the cell is solubilized in detergent and purified on an affinity column. The purified membrane protein is then mixed with the desired lipid to form the ternary complex. The detergent is gradually removed from the ternary complex using various techniques to reconstitute the membrane protein in liposomes.

Figure 6. – correlation spectra of (a) uniformly labeled KcsA–Kv1.3 in the presence (green) and absence (red) of KTX, and (b) uniformly labeled SRII before (black) and after addition (green) of TrII. In (b), specific amino acids are indicated.