Comprehensive mass spectrometric structural analysis was performed to elucidate the structure of a hetero-hexameric protein complex, TNH. SID/IM experiments resulted in a contact map of different subunits in this complex. The contact information, together with the collisional cross-section constraints, constructed a coarse-grained model for the TNH hexamer. Later on, covalent labeling together with protein complex homology modeling was utilized to propose possible atomic level structures of TNH hexamer. The combined results from different mass spectrometry approaches and computational modeling provide a robust framework for analysis of protein complexes.
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