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![[Figure 1]](rr5237fig1mag.jpg)
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Figure 1
AlphaFold models of C. elegans α2/β5. (a) Models of Ceα2/β5 predicted by AlphaFold in the monomer mode for α2 and β5 joined computationally by an artificial linker (left) and in the multimer mode for α2 and β5 separately. These ribbon drawings are colored by pLDDT score using the color scheme from the AlphaFold Protein Structure Database as shown below. (b) AlphaFold model for residues with pLDDT > 70, which are essentially identical within the monomer and multimer models. Here, the ribbon drawing for α2 is colored red and that for β5 is green. (c) The top-rated AlphaFold models from the monomer mode (S0) and the multimer mode (M0) are compared with the other four models (S1–S4 and M1–M4) produced for the respective mode. For each comparison, the r.m.s.d. is plotted as a function of decreasing pLDDT score in bins of N + 10 ≥ pLDDT > N. |
![[Figure 1]](rr5237fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
