Fig. 5: In silico fibril stability in ATTRv-I84S amyloidosis fibrils. | Nature Communications

Fig. 5: In silico fibril stability in ATTRv-I84S amyloidosis fibrils.

From: Structural polymorphism of amyloid fibrils in ATTR amyloidosis revealed by cryo-electron microscopy

Fig. 5

a, b Comparison of average stabilization energies of solvation between ATTR fibrils and all amyloid fibrils reported in the Amyloid Atlas 202328. a Stabilization energies by chain. b stabilization energies by residue. ATTR fibrils are significantly more stable than the other amyloid structures, considering the energies of both chains and residues. n = 7 (ATTR fibrils, ours and from others21,22,23). n = 86 (others). Data are presented as Box-and-whisker plots. The horizontal line in each box represents the median value. The 25th–75th percentiles represent the endpoints of the box, with whiskers at minimum and maximum values. Nonparametric two-sided Mann–Whitney t test was used for analysis. P values are included in the graphs. Graphed data are provided in a Source data file. c Representation of stabilization energies per residue of cardiac ATTRv-I84S fibrils determined in this study. Strongly stabilizing side chains are colored red, and destabilizing side chains are colored blue.

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