Surface-induced dissociation (SID) causes native-like protein complexes to dissociate along the weakest subunit interfaces, providing information about subunit stoichiometry and connectivity, assuming that no intertwined subunits exist and/or that restructuring is not a necessary path to dissociation. However, when isCA causes rearrangement to a non-native-like structure, the protein complexes will no longer produce nativelike SID fragmentation patterns. By this we mean that protein complexes will not dissociate through pathways that indicate their native-like topology, subunit connectivity, etc. Work published by the Wysocki lab in 2015 illustrates this point. As protein complexes were subjected to various degrees of isCA, they underwent structural rearrangement that was reflected in the SID spectrum. Collision-induced dissociation (CID) was not able to detect these structural rearrangements because the CID products are typically a highly charged monomer and the complementary (N-1mer) subunit, which does not possess a native-like topology. Thus, SID proved to be a useful probe of source-induced structural rearrangements and can be used to tune isCA to maintain native-like structures.