Supplementary Figure 5: Scatter plots of contour lengths and unfolding forces for all the titin fragments studied, with kernel density estimates shown as lines.
From: Mechanochemical evolution of the giant muscle protein titin as inferred from resurrected proteins
Data collection for each protein is n=374 for LTCA, n=614 for LSCA, n= 407 for LMCA, n= 366 for LPMCA, n= 409 for zebra finch, n= 375 for chicken, n= 263 for orca, n= 341 for rat and n= 347 for human titin fragment. Blue bars indicate force and length of domains with no disulfide bonds. Red bars represent domains with disulfide bridges. Domains that do not contain disulfide bonds and are thus fully extended are represented in blue, whereas those showing disulfide bonds are represented in red and display lower mechanical resistance. In the last graph, the average unfolding forces of ancestral and extant species are shown with square and circles, respectively. Unfolding forces in both types of domains increase when the percentage of experimental disulfide bonds is higher, following a linear relationship.
