Fig. 3.
Fig. 3. Plot of the backbone amide chemical-shift changes (Δδ) against residue numbers in Spα1-156Arg45Ser and Arg45Thr relative to Arg28/Arg45, and missing resonances in Arg45Ser. / Sample identity is indicated at the top of each plot. Normalized chemical-shift changes in the top 2 plots were calculated as described in “Materials and methods.” Residues that could not be identified because of changes in the mutant spectra (residues 44, 45 in Arg45Thr; and 42, 45 in Arg45Ser) are left blank. The bottom plot notes resonances missing in the Arg28Ser HSQC spectrum, as compared with that of the native peptide.

Plot of the backbone amide chemical-shift changes (Δδ) against residue numbers in Spα1-156Arg45Ser and Arg45Thr relative to Arg28/Arg45, and missing resonances in Arg45Ser.

Sample identity is indicated at the top of each plot. Normalized chemical-shift changes in the top 2 plots were calculated as described in “Materials and methods.” Residues that could not be identified because of changes in the mutant spectra (residues 44, 45 in Arg45Thr; and 42, 45 in Arg45Ser) are left blank. The bottom plot notes resonances missing in the Arg28Ser HSQC spectrum, as compared with that of the native peptide.

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