IscS Kinetics in Native Mass Spectrometry Buffers Reveal Key Physiochemical Properties that Influence Enzyme Activity.

ABSTRACT: Investigations of protein function and interactions with native mass spectrometry (MS) have yielded significant insights into protein dynamics, transient reaction intermediates, and pharmacokinetic targets. The pursuit of these studies and their outcomes depend on the preparation of protein samples in a manner able to support native conformation, active site chemistry, and protein-ligand interactions. Although ammonium acetate is a commonly utilized volatile buffer in MS-based analyses, the gap in buffer capacity near physiological pH calls into question whether this or other volatile buffer solutions are able to facilitate native conformation and protein-ligand interactions in the gas phase. We report enzymatic activity of the cysteine desulfurase IscS in four volatile buffer solutions co

SUBMITTER: Oney-Hawthorne SD 

PROVIDER: S-EPMC12784406 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature