Figure 3 | Scientific Reports

Figure 3

From: Solution structure of the autophagy-related protein LC3C reveals a polyproline II motif on a mobile tether with phosphorylation site

Figure 3

15N transverse (A) and longitudinal (B) relaxation rates and {1H}15N heteronuclear NOE values (C) measured at 800 MHz and 20.0 °C, and generalized order parameters S2 of the sub-nanosecond backbone amide motion (D). Dashed horizontal lines in (A,B) represent the average values over the ordered region (residues 18–120). {1H}15N values below 0.65 (dashed horizontal line in (C)) indicate increased internal mobility29. Experimental order parameters S2 obtained from 15N relaxation analysis (blue) are compared with order parameters predicted from the Random Coil Index (RCI)33, SRCI2 (red circles), calculated with the default parameters as implemented in TALOS-N80,81. The regular secondary structure elements are indicated above the graph.

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