Membrane proteins, site-directed solid-state dynamics

Site-directed solid state NMR spectra of [3- C]Ala- and [l- C]Val-labelled bacteriorhodopsin as a typical membrane protein in lipid bilayers, have been reported. Well-resolved NMR signals were observed for monomeric [3- C]Ala- bacteriorhodopsin in egg phosphatidylcholine bilayer at ambient temperature, although several NMR signals from the loops and transmembrane a-helices were still suppressed. The NMR results were used to elucidate the effect of 2D array formation on the backbone dynamics of membrane proteins in lipid bilayers. 

H. Saito, J. Mikami, S. Yamaguchi, M. Tanio, A. Kira, T. Arakawa, K. Yamamoto, S. Tuzi, Site-directed solid-state NMR studies on membrane proteins strategy and goals toward revealing conformation and dynamics as illustrated for C-labeled bacteriorhodopsin, Magn. Reson. Chem. 42 (2004) 218—230. 

H. Saito, K. Yamamoto, S. Tuzi, S. Yamaguchi, Backbone dynamics of membrane proteins in lipid bHayers the effect of two dimensional array formationas revealed by site-directed solid-state C NMR studies on [3- C]Ala- and [l- C]Val-labeled bacterorhodopsin, Biochim. Biophys. Acta 1616 (2003) 127-136. 

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