Fig. 1
From: NMR structural analysis of the yeast cytochrome c oxidase subunit Cox13 and its interaction with ATP
Backbone chemical shift assignment of Cox13 in DPC micelles. a 900 MHz 2D 1H-15N TROSY-HSQC spectrum of 0.4 mM [15N, 13C]-labeled Cox13 in 20 mM NaPi pH 6.5, 50 mM L-Arg, 50 mM L-Glu, 1 mM DTT, and 30 mM DPC recorded at 40 °C. The assignment of each peak is given with residue one-letter code and sequence number. b For clarity, the central region of the spectrum is enlarged. c The Cα secondary chemical shifts of Cox13 in DPC micelles plotted versus the amino acid sequence. Consecutive positive secondary chemical shifts indicate α-helical secondary structure. d Protein sequence alignment for Cox13 in selected homologs. Positions of experimentally determined α-helices are indicated above the alignment. Pink shading indicates conserved residues across the homologs