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In amyotrophic lateral sclerosis (ALS) and several other neurodegenerative disorders, TDP\u201043 undergoes aberrant phase transitions, forming insoluble amyloid aggregates, including fibrils composed of solely its intrinsically disordered C\u2010terminal domain (CTD). Despite its central role in disease, the conformational dynamics of the CTD remain poorly understood due to its heterogeneous and transient conformational landscape. Here, we employ native ion mobility\u2010mass spectrometry (IM\u2010MS) using nanopipette sub\u2010micron nano electrospray ionization (nanoESI) emitters to characterize the conformational landscape of wild\u2010type and ALS\u2010associated TDP\u201043 CTD variants (Q331K and R361S) under different solution conditions. Our data suggest that mutations and salt concentration modulate the CTD's conformations. Combined with thioflavin T fluorescence, light scattering, and microscopy, we reveal that these conformational shifts correlate with altered amyloid assembly kinetics and propensity to form condensates. Notably, the Q331K variant, which has a mutation in the transient \u03b1\u2010helical region in the CTD, has reduced propensity to form biomolecular condensates but can undergo amyloid assembly in the absence of condensate formation, suggesting that sequence alterations in this \u03b1\u2010helical region can tune the molecular mechanism of amyloid assembly. This study demonstrates the power of IM\u2010MS in probing disordered proteins and reveals mechanistic insights into how disease\u2010associated mutations differentially tune TDP\u201043 CTD amyloid assembly mechanisms.<\/jats:p>","DOI":"10.1002\/pro.70565","type":"journal-article","created":{"date-parts":[[2026,4,13]],"date-time":"2026-04-13T09:59:15Z","timestamp":1776074355000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["An\n                    <scp>ALS<\/scp>\n                    \u2010associated mutation in the C\u2010terminal \u03b1\u2010helix of\n                    <scp>TDP<\/scp>\n                    \u201043 uncouples condensate formation and amyloid assembly"],"prefix":"10.1002","volume":"35","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-9876-1400","authenticated-orcid":false,"given":"Emily J.","family":"Byrd","sequence":"first","affiliation":[{"name":"Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences University of Leeds  Leeds UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joel A.","family":"Crossley","sequence":"additional","affiliation":[{"name":"Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences University of Leeds  Leeds UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chalmers C. 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