Intrinsically Disordered p53 and Its Complexes Populate Compact Conformations in the Gas Phase

摘要

The use of ion mobility mass spectrometry (IM-MS) to study the topology of proteins and their complexes is attracting considerable attention. Under the appropriate conditions results have shown that unique insight can be gained for intractable systems such as protein aggregates, viral cap-sids, and membrane complexes. From fundamental studies of peptides and proteins it is clear that folded structure, present in bulk solution, upon transfer into the gas phase, can retain native-like compact states but may unfold when activated or stored. Similarly assemblies of globular proteins studied by IM-MS have been found to retain defined topological arrangements, with unfolding of subunits being linked to activation in the gas phase. High charge states of proteins and their complexes in the gas phase are associated with extended unfolded structures, analogous to unfolding processes induced by protonation in solution.