Using nIM-TDMS we have demonstrated the usefulness of a conformation-specific approach for direct nTDMS analysis of proteins and their complexes. Instead of sampling across the entire conformational landscape or relying on post-processing extraction methods, we can selectively isolate specific protein conformers within the instrument, which enables us to link the intrinsic structural and proteoform information obtained from nTDMS experiments direcly to specific protein conformations. Our conformation-specific approach is therefore perfectly placed to provide structural insights and component characterization for proteins and their complexes all within the same experiment, making it invaluable in enabling a true biological understanding of systems where proteins exhibit multiple structures, and transient or low abundant structural intermediates. We believe that nIM-TDMS has great potential in the structural characterization of traditionally challenging families of proteins and complexes, such as intrinsically disordered proteins, glycoproteins, membrane proteins, or proteins that are prone to misfolding and aggregation. nIM-TDMS can also provide amino acid level, conformation specific data for integrative structural biology workflows, supplying information which is currently underused due to difficulties in obtaining it by classic structural or biophysical methods, but which is required to provide a truly accurate picture of the systems studied.