Structural differentiation of protein charge state conformers via gas-phase ion/ion cross-linking mass spectrometry.

ABSTRACT: Determining structures of multiply charged protein ions in mass spectrometry is critical for understanding the relationship between condensed-phase protein structures found in biological environments and gas-phase structures produced during electrospray ionization (ESI). The determination of collision cross-sections (CCSs) via ion mobility-mass spectrometry (IM-MS) has been used to study conformational changes as a function of protein charge state; however, this approach provides limited structural information on the overall topology of analytes. Recently developed gas-phase cross-linking mass spectrometry (XL-MS) performed via ion/ion reactions can probe local tertiary structures, providing an additional dimension to MS-based gas-phase structural biology studies. Herein, we demonstrate th

SUBMITTER: Kang WY 

PROVIDER: S-EPMC12657030 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature