Figure 2: A mass spectrum of solution and gas-phase dissociation products of the cATPase. | Nature Communications

Figure 2: A mass spectrum of solution and gas-phase dissociation products of the cATPase.

From: Comparative cross-linking and mass spectrometry of an intact F-type ATPase suggest a role for phosphorylation

Figure 2

At high activation energy, micelle-stripped complexes are observed, with those between 9,000 and 11,000 m/z assigned to complexes formed in solution. First and second generation CID products are formed by the loss of one or two subunits observed between 12,000 and 14,000 m/z, and 16,000 and 25,000 m/z, respectively. The spectrum represents a typical cATPase mass spectrum from at least three replicates. A schematic representation of the solution and gas-phase dissociation pathways is shown (inset). Brackets denote complexes identified in mass spectra recorded under different conditions.

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