5). Pattern labeling reduces the number of CCI-779 correlation signals and decreases the linewidth of these signals compared to the uniformly labeled samples, which enables to resolve the narrowly distributed correlation signals of the backbone carbons and nitrogens involved in the long α-helical transmembrane segments. [1,2,3,4–13C], [1,4–13C] and [2,3–13C] succinic acid were chemically labeled and used for the biosynthetic preparation of site-directed isotopically 13C enriched LH2 complexes from the Rhodopseudomonas acidophila strain 10050. 2D PDSD correlation learn more spectroscopy was used to show that carbonyl carbons in the

protein backbone were labeled by [1,4–13C]-succinic acid, while the Cα and Cβ carbons of the residues were labeled by [2,3–13C]-succinic acid in the growth

medium (van Gammeren et al. 2004). In addition, leucine and isoleucine residues can be labeled using a uniformly labeled amino acid mixture in the medium (van Gammeren et al. 2004). Fig. 5 In the upper panels two regions from homonuclear 13C–13C PDSD correlation spectra collected from 2,3-LH2 (red) and AA-LH2 (black) are shown. The upper left panel contains cross peaks between aliphatic and carbonyl carbons, while the upper right panel shows correlations between sidechain aliphatic carbons. In the upper right panel the aliphatic responses are shown. In the middle panel, the aliphatic region of the NCACX spectra of 2,3-LH2 (red) and AA-LH2 (black) are shown. Finally, in the lower panel the NCACX spectrum of a 1,2,3,4-LH2 sample is shown The pattern Erastin mouse labeling allows for the residual assignment of the LH2 α-helical transmembrane protein complex. Correlations between nearby residues and between residues and the labeled BChl a cofactors, provided

by Interleukin-3 receptor the 13C–13C correlation experiments using a 500 ms spin diffusion period, were utilized to arrive at sequence specific chemical shift assignments for 76 residues of the 94 residues of the monomeric unit of the LH2 complex. An example of the sequence specific assignment of LH2 is shown in Fig. 5. Here the LH2 were labeled with either [2,3-13C]-succinic acid (2,3-LH2), [1,2,3,4-13C] succinic acid (1,2,3,4-LH2) or with uniformly 13C-labeled amino acids (AA-LH2). In the upper left part of Fig. 5, a few responses are observed for 2,3-LH2, belonging to H, Q and E residues. The responses from AA-LH2 in the carbonyl area are from I, L, A, G and V. The blue spectrum in the carbonyl region comprises carbonyl responses from 1,2,3,4-LH2. The dashed lines in the upper right panel indicate correlations involving the αT38 and four P residues for the 2,3-LH2, and correlations involving βI16 for the AA-LH2. Here we follow the notation in (van Gammeren et al. 2005b).