Figure 2 | Scientific Reports

Figure 2

From: Expression of Ice-Binding Proteins in Caenorhabditis elegans Improves the Survival Rate upon Cold Shock and during Freezing

Figure 2

Model structure and TH activities of AnpIBP1a and its mutants. (A) Predicted structure of AnpIBP1a coloured from blue (N-terminus) to red (C-terminus). The β-sheets of AnpAFP1a were usually stacked in the order of β1-β6-β5-β4-β3-β2, which is similar to the order in other microbial IBPs, such as TisIBP634. (B) Upper view of (A). Triangular cross-section showing three parallel β-sheets, namely, A-face, B-face, and C-face. Mutated residues are shown in blue (T156Y) and red (N55D). Tyrosine was used to determine the ice-binding site (IBS), which is known to affect the antifreeze activity. Asn55 was mutated to an aspartic acid residue to remove N-glycan, which plays an unknown role. (C) TH activities of AnpIBP1a, AnpIBP1a_N55D, and AnpIBP1a_T156Y plotted as a function of the protein concentration (µM). In each assay, n = 3. Error bars indicate the standard error of the mean. The error bars of AnpIBP1a_T156Y are shorter than the size of the symbol.

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