Application of Multiple Length Cross-linkers to the Characterization of Gaseous Protein Structure.

ABSTRACT: The speed, sensitivity, and tolerance of heterogeneity, as well as the kinetic trapping of solution-like states during electrospray, make native mass spectrometry an attractive method to study protein structure. Increases in the resolution of ion mobility measurements and in mass resolving power and range are leading to the increase of the information content of intact protein measurements and an expanded role of mass spectrometry in structural biology. Herein, a suite of different length noncovalent (sulfonate to positively charged side chain) cross-linkers was introduced via gas-phase ion/ion chemistry and used to determine distance restraints of kinetically trapped gas-phase structures of native-like cytochrome c ions. Electron capture dissociation allowed for the identification of cros

SUBMITTER: Cheung See Kit M 

PROVIDER: S-EPMC9532380 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature