Abstract

Proteins typically carry out their biological function as parts of multimeric complexes. Recent advances in mass spectrometry (MS) have enabled the study of these complexes in their native form in the gas phase (nMS). These experiments can provide accurate molecular weight and stoichiometric information, while the study of complex dissociation in tandem MS with an activation step can facilitate the exploration of the architecture of the complex. Surface induced dissociation (SID) has emerged as an ideal activation step for tandem MS that helps reveal the architecture of protein complexes.

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