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Tandem ion mobility spectrometry reveals that glycosylation does not alter the conformational heterogeneity of a monoclonal antibody. 

Cellular processes are usually carried out collectively by the entirety of all proteins present in a biological cell, i.e., the proteome. Mass spectrometry-based methods have proven particularly successful in identifying and quantifying the constituent proteins of proteomes, including different molecular forms of a protein. Nevertheless, protein sequences alone do not reveal the function or dysfunction of the identified proteins. A straightforward way to assign function or dysfunction to proteins is characterization of their structures and dynamics. However, a method capable to characterize detailed structures of proteins and protein complexes in a large-scale, systematic manner within the context of cellular processes does not yet exist. Here, we discuss the potential of tandem -ion mobility/mass spectrometry (tandem-IM/MS) methods to provide such ability. We highlight the capability of these methods using two case studies on the protein systems ubiquitin and avidin using the tandem-TIMS/MS technology developed in our laboratory and discuss these results in the context of other developments in the broader field of tandem-IM/MS. 

This review focuses on the instrumental development and potential applications of Tandem-Trapped Ion Mobility Spectrometry/Mass Spectrometry (tTIMS/MS) for protein structure elucidation.