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ABSTRACT: Rationale
To perform native mass spectrometry (MS) studies, there are a limited number of volatile and electrospray ionization (ESI)-MS compatible solutions, such as ammonium bicarbonate and ammonium acetate (AA). These solutions could induce the unfolding of proteins due to the formation of CO2 bubbles or induced acidification during ESI. Hence, it was important to introduce a buffer suitable to preserve the native form of proteins while simulating physiological conditions.Methods
The 4-ethylmorpholinium/acetate (4EM/A) buffer was compared to AA for the analysis of proteins and protein complexes with mass ranges from 5 to 103 kDa and isoelectric points (pI) between 3 and 11. The evaluations were conducted by comparing the native-MS profiles, CCS values, arrival
SUBMITTER: Hadavi D
PROVIDER: S-EPMC12010238 | biostudies-literature | 2025 Jul
REPOSITORIES: biostudies-literature