Figure 5: Sensitivity analysis of the predicted co-translational folding curve of ΔC SFVP to changes in the number of residues that fit inside the ribosome, kA,i, kF,i and kU,i | Nature Communications

Figure 5: Sensitivity analysis of the predicted co-translational folding curve of ΔC SFVP to changes in the number of residues that fit inside the ribosome, kA,i, kF,i and kU,i

From: Accurate prediction of cellular co-translational folding indicates proteins can switch from post- to co-translational folding

Figure 5

(a) Co-translational folding curves calculated using kF,i values of 0.02, 2, 20 or 200 s−1 in equation (2) are plotted alongside the experimental time course (blue squares, panels a, b, c, and d. (b) Co-translational folding curves calculated using kU,i values of 43.0, 4.34 × 10−4, 4.34 × 10−5 and 4.34 × 10−6 s−1. (c) Co-translational folding curves for the cases of the ribosome exit tunnel including 20 (green triangles), 30 (red squares) or 40 (blue diamonds) amino acids. (d) Co-translational folding curves calculated using global codon translation rates of 7.6 (purple diamonds), 3.9 (red triangles) or 1.9 AA per second (green circles).

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