One challenge in interpreting results from mass spectrometry experiments is that the structures of protein complexes in the gas phase may differ from those in solution. Here, we investigate the stabilization properties of trisH+, a non-volatile electrospray buffer component, by experimentally characterizing the unfolding and dissociation of three gas-phase tetrameric protein complexes. We find that trisH+ preferentially stabilizes the compact native-like state of these protein complexes.
Gas-Phase Protein Assemblies: Unfolding Landscapes and Preserving Native-Like Structures Using Noncovalent Adducts Joanna Freekea, Matthew F. Bush, Carol V. Robinson, Brandon T. Ruotolo. Chem. Phys. Lett. 2012, 524, 1-9.