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. 2010 Feb 5;285(15):11235–11242. doi: 10.1074/jbc.M110.102962

FIGURE 3.

FIGURE 3.

The C-terminal domain of Spy0128 E258A extends upon the application of force. A diagram of the protein construct employed, (I27-Spy0128-E258A)2-I27, is shown (see also legend to Fig. 1). The mutation E258A abolishes the formation of the isopeptide bond at the C-terminal domain of Spy0128 (in the diagram, this is denoted by an open circle). A, typical force-extension trace for (I27-Spy0128-E258A)2-I27 is shown in blue. The peaks marking the unfolding of the Spy0128 C-terminal domains in the polyprotein are labeled with an asterisk. The increment in contour length after the Spy0128 unfolding events is calculated from the worm-like chain fits shown in red. Inset: the unfolding of the C-terminal domain through an intermediate is shown. B, histogram of the unfolding forces for the C-terminal domain in Spy0128 E258A (n = 135). The solid line corresponds to a Gaussian fit of the experimental data. C, histogram of the ΔLc associated with the unfolding of the C-terminal domain in Spy0128 E258A (n = 169). Solid lines are Gaussian fits to the data.