Mass Spectrometry of Proteins and Protein Complexes Electrosprayed in the Presence of Common Biological Buffers Using Theta Emitters.

ABSTRACT: Salt-protein interactions are essential in biology. However, the presence of nonvolatile salts at physiologically relevant concentrations (e.g., 150 mM NaCl) is detrimental to mass analysis by electrospray ionization mass spectrometry (ESI-MS). Nonvolatile salts tend to compromise ionization yields and, when analyte ions are observed, lead to peak broadening and shifts to higher mass. Ultimately, these phenomena yield lower signal-to-noise (S/N) ratios and, in the worst-case scenario, totally suppress the formation of the analyte ions of interest. For these reasons, the sample is generally desalted before mass analysis. Direct sample introduction into the mass spectrometer is widely used in "native" ESI-MS, where the preservation of protein interactions is a priority. Unfortunately, native

SUBMITTER: Baez Bolivar EG 

PROVIDER: S-EPMC12764350 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature