Incorporation of Ion Mobility (IM) into the nTDMS workflow is one approach that can provide added value for users looking to link top-down fragmentation data to conformational elements of proteins. IM is able to provide a low resolution readout of protein structure, which if used in sequence with a dissociation method directly links structure to fragmentation. As such, combining these two powerful methods goes a long way in verifying which structure(s) are present in any given nTDMS experiment, thus further validating structural interpretation of the results. Such workflows are particularly beneficial for proteins thought to be highly disordered, or those known to exist in multiple conformations. Similarly, the approach is particularly fruitful in the case of protein misfolding, allowing distinctive features of incorrectly folded proteins to be easily distinguished from the correctly folded analogue.