However, the drift time decreases to a new stable feature at cone voltages above 120 V. This suggests that isCA causes the cyclic protein complex to collapse. The ultimate effect of isCA on SID is seen in Figure , which shows a few selected SID products. The full plot with all SID products can be seen in Figure . At cone voltages below 60 V and with a fixed SID energy of 1050 eV, the most prevalent SID products are the monomer, pentamer, and hexamer subunits, followed by residual 11mer precursor. As seen in Figure (blue bars), the other complementary oligomeric pairs (1/10, 2/9, 3/8, 4/7) seem to have complementary signal intensities, which should be due to native-like fragmentation. As isCA becomes more aggressive Figure shows a significant shift in SID behavior at a cone voltage of 50 -70 V, a trend that seems to level off by a cone voltage of 100 V, when the CIx plot barely starts to suggest the possibility of structural rearrangement. The monomer signal is this region, cone voltage 50 -100 V, appears similar to the monomer trend for SA (Figure ) and CRP (Figure ), which suggests that secondary fragmentation due to energy deposition from isCA and SID is at play here as well. As seen in Figure (red bars) at the highest cone voltage (most severe isCA), the SID product distribution shifts towards lower oligomeric states, more reflective of non-native fragmentation behavior as captured for the 21+ charge state at the same SID energy (Figure gold bars).