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. 2021 Jun 8;22(12):6190. doi: 10.3390/ijms22126190

Figure 1.

Figure 1

Conserved segments, charge distribution, in silico, and experimental α-helical propensities of the ERD14 protein. Conserved regions: Ka-, Kb-, Kc- (blue), S- (yellow), Chp- (green), and H-segment (red) indicated in the sequence of ERD14. In addition to individual charges above the regions, net charge/number of charged side chains/length of regions summed up. Underlined letters show residues with α-helical propensity calculated from nuclear magnetic resonance (NMR) chemical shifts [9,16] by δ2D method [17]. Below the residues, H indicates the α-helical propensity estimated by in silico PredictProtein analysis [18,19,20].