Fig. 1: dsA2 is stable at very low dipeptide concentrations. | Nature Communications

Fig. 1: dsA2 is stable at very low dipeptide concentrations.

From: Structures of peptide-free and partially loaded MHC class I molecules reveal mechanisms of peptide selection

Fig. 1

Thermal denaturation of A2 in the presence of increasing concentrations of GM measured by nanoDSF (tryptophan fluorescence). a, b First derivatives of the F350/F330 (ratio of fluorescence emissions at 350 and 330 330 nm) curves for wtA2 a and dsA2 b with the maxima reporting the melting temperatures (Tm). The concentration of GM (in mm) is indicated in rainbow colors from red (maximum, 100 mm) to blue (lowest, 0.05 mm). The arrow points to the transition of the dsA2 heavy chain that is visible even at very low dipeptide concentration. c Scatter plot of the Tm obtained for the A2 heavy chain (first unfolding event in A) as a function of GM concentration (mmΜsmall M).

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