Heteronuclear multidimensional NMR spectroscopy of solubilized membrane proteins: resonance assignment of native bacteriorhodopsin
M. Schubert, M Kolbe, B. Kessler, D. Oesterhelt, P. Schmieder
Chembiochem (2002) 3, 1019-1023
A solution state NMR study of the native integral membrane protein bacteriorhodopsin is presented. Bacteriorhodopsin was used as a model system for proteins consisting of seven transmembrane helices. Experiments using TROSY-type NMR techniques were applied to uniformly 2H/15N- and 2H/13C/15N-labeled samples solubilized with dodecylmaltoside. The assignment of 81 out of 248 residues, mainly in the loop regions, is given. Subsequently, structural and dynamic information is derived from the data.
supporting material (pdf)