Ion Mobility-Mass Spectrometry Reveals Conformational Changes in Charge Reduced Multiprotein Complexes

• DOI: 10.1007/s13361-011-0204-y
• Publication Date: 2011-07-15T19:08:52Z
• Authors: Russell E. Bornsc...; Suk-Joon Hyung; Brandon T. Ruotolo
• Keywords: Multiprotein complex; Ion-mobility spectrometry; Fragmentation

Characterizing intact multiprotein complexes in terms of both their mass and size by ion mobility-mass spectrometry is becoming an increasingly important tool for structural biology. Furthermore, the charge states protein can dramatically influence information content gas-phase measurements performed. Specifically, complex state has a demonstrated upon conformation, resolution, mobility dissociation properties assemblies collisional activation. Here we present first comparison charge-reduced generated solution additives ion-neutral reaction chemistry. While reduction mechanism methods undoubtedly similar, significant activation required to reduce using additive strategy employed here. This step act unfold complexes, making data difficult correlate with solution-phase structures topologies. We use chart such conformational effects range multi-protein demonstrate that approaches based on chemistry consistently produce having compact, 'native-like' geometries while same molecules added generate significantly unfolded identical states.