Solid-state NMR analysis of membrane protein complexes with 7-transmembrane helices

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Solid-state NMR enables the structural determination of biological molecular complexes in unoriented solids. We verified the usefulness of magic-angle spinning solid-state NMR based on dipolar and J couplings for the structural analysis of ^<13>C uniformly labeled biomolecular complexes. We applied solid-state NMR to halorhodopshin, mastoparan-X and 159-redisue transducer protein pHtrII in lipid bilayers. Solid-state NMR provided the detailed structure of mastoparan-X with membranes by combining NMR constraints with replica exchange molecular dynamics simulation using implicit membrane environment. This method was applied to NMR analysis of larger membrane proteins. ^1H-^<13>C correlations of mobile segments of pHtrII were analyzed.