Native-like ions, which are generated using electrospray ionization of proteins, nucleic acids, lipids, and other biological molecules in aqueous solutions, can retain noncovalent interactions in the gas phase that were present in the original solution. Ion mobility mass spectrometry measurements of native-like ions are now used in applications towards structural biology and biophysics. Therefore, an accurate understanding of the fidelity between the structures of proteins in solution and protein ions in the gas phase is critical to experiments that use gas-phase measurements to infer structures in solution. I will report recent experiments in my lab that made use of ion mobility, ion chemistry, energy-dependent activation, and time-dependent kinetics in order to probe the structures and structural evolution of protein ions in the gas phase. I will then discuss the implications of these results to the interpreation of structural mass spectrometry data.

Interpreting the collision cross sections of proteins: Insights from Ion mobility, unfolding, and folding of ions in the gas phase

256th National Meeting (2018)

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