Abstract

Abstract Solid state NMR spectra from uniformly 13C, 15N enriched bacteriorhodospin (bR) purified from H. sali-narium were acquired at 18.8 T using magic angle spinning methods. Isolated resonances of 2D 13C-13C spectra exhibited 0.50–0.55 ppm line-widths. Several amino acid types could be assigned, and at least 12 out of 15 Ile peaks could be resolved clearly and identified based on their characteristic chemical shifts and connectivities. This study confirms that high resolution solid state NMR spectra can be obtained for a 248 amino acid uniformly labeled membrane protein in its native membrane environment and indicates that site-specific assignments are likely to be feasible with heteronuclear multidimensional spectra.