Collision cross section (a) values of gas-phase ions of proteins and protein complexes are used to probe the structures of the corresponding species in solution. Ions of many proteins exhibit increasing a-values with increasing charge state but most Omega-values calculated for protein ions have used simple collision models that do not explicitly account for charge. Here we use a combination of ion mobility mass spectrometry experiments with helium gas and trajectory method calculations to characterize the extents to which increases in experimental Omega-values with increasing charge state may be attributed to increased momentum transfer concomitant with enhanced long-range interactions between the protein ion and helium atoms. Ubiquitin and C-to-N terminally linked diubiquitin ions generated from different solution conditions exhibit more than a 2-fold increase in a with increasing charge state. For native and energy-relaxed models of the proteins and most methods for distributing charge, a-values calculated using the trajectory method increase by less than 1% over the range of charge states observed from typical solution conditions used for native mass spectrometry. However, the calculated Omega-values increase by 10% to 15% over the full range of charge states observed from all solution conditions. Therefore, contributions from enhanced ion induced dipole interactions with increasing charge state are significant but without additional structural changes can account for only a fraction of the increase in a observed experimentally. On the basis of these results, we suggest guidelines for calculating Omega-values in the context of applications in biophysics and structural biology.