Fig. 2: The NMR characterization of membrane-bound CD260-290. | Nature Communications

Fig. 2: The NMR characterization of membrane-bound CD260-290.

From: PD-L1 degradation is regulated by electrostatic membrane association of its cytoplasmic domain

Fig. 2

a 1H-15N TROSY-HSQC spectrum of CD260-290 in POPG/DH6PC bicelles with backbone resonances assigned. The spectrum was recorded at 1H frequency of 600 MHz using [15N, 2H]-labeled protein. b Lipid NOEs from CD260-290 in POPG/DH6PC bicelles. Strips from 3D 15N-edited NOESY-TROSY-HSQC (τNOE = 200 ms) spectra recorded using 0.8 mM [15N, 2H]-labeled CD260-290 in the bicelles with protonated POPG and deuterated DH6PC show the NOEs exclusively between backbone amide protons of CD260-290 and methyl protons or methylene protons of lipid acyl chains of POPG, and the NOEs between backbone amide protons of CD260-290 and glycerol protons of lipid head groups and water protons (*), mostly for the residues in the N-terminal half of the protein. The spectrum was recorded at 1H frequency of 900 MHz. c Strips from the same experiment mentioned above showed the NOEs from the side chains of three arginine residues to the lipid acyl chains and headgroups of POPG.

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