Ion mobility-mass spectrometry (IM-MS) is a powerful tool for structural biology with the ability to simultaneously assess the structure, topology, dynamics, and composition of large heterogeneous multi-protein complexes at low micro-molar concentrations. However, one of the challenges in using IM-MS is that the structures of protein complexes in the gas phase can differ from those in solution as a consequence of ionization, desolvation, transport, and analysis over a range of time scale and energies. Thus, a general means must be identified to stabilize protein structures in the gas phase. Our approach involves stabilizing protein structure through the addition of inorganic cations and anions, or by crosslinking the intact complex (in collaboration with Dr. Philip Andrews (UM Biological Chemistry). Collision-induced dissociation (CID) and collision-induced unfolding (CIU) profiles of multi-protein systems could be used to quantitatively determine the increase in gas-phase protein stability.
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