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

A combination of ion mobility/mass spectrometry, solution and gas phase crosslinking reactions, and solution and gas phase molecular modeling was used to determine solution and gas phase conformational preferences of the model IDP alpha synuclein. 

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.