In the last nIM-TDMS workflow (Figure red line), it is possible to characterize the ligands that are involved in single-conformation protein:ligand complexes, in an approach similar to that of the native-omics workflow first described by Gault and colleagues, but for the first time using QToF instrumentation. The workflow for this (Figure ) involves native introduction of the protein:ligand complex into the mass spectrometer, following by m/z selection of a single protein:ligand species. The complex is then mobility separated, and a single conformation of the complex isolated in the pre-array store, as demonstrated for a calmodulin-melittin complex in Figure . The complex is then collisionally dissociated by application of activation upon its re-injection from the pre-array store into the mobility cell, causing it to break down into its component parts. Tandem IM can then be applied to isolate only the mobility region associated with the peptide ligand, Figure , allowing for ligand identification by top-down MS using either ECD or CID, Figure . In this way, unlike the native-omics approach, in which multi-stage MS experiments are performed based upon a m/z isolation, our workflow instead performs species selection based upon mobility, overcoming the MS-in-space limitations traditionally associated with QToF instrumentation. As is demonstrated, this mobility selection of specific conformational species works particularly well for peptides like melittin (Figure ) , as they occupy significantly different arrival times compared to the free protein or protein:ligand complex. We expect similar behaviors for ligand-types such as peptides, organic molecules, and lipids, given their differing mobility compared to proteins, opening up the door to applying this method for the identification of these ligands within protein complexes. Subsequent fragmentation of the ligand by ECD or CID can then be performed. The application of activation to release the ligand is predicted to negate the relevance of any structural findings from this workflow, however suffi-cient coverage is achieved to enable successful identification of melittin from the calmodulin-ligand complex (Figure ). Given this level of coverage, we foresee the approach being particularly applicable for identifying unknown ligands from within native complexes, for example endogenous complexes where the specific ligand bound might otherwise not be clear due to lack of previous characterization. As with similar approaches, however, such endeavors would require knowledge of the ligand fragmentation patterns to aid identification, and whilst these are well reported for peptides and glycans, they become considerably more variable or less informative when wanting to identify small molecules or lipids.