Authors
Samantha Sarni, Edric Choi, Lien B Lai, Mengxuan Jia, Benjamin J Jones, Alyssa Q Stiving, David H Russell, Venkat Gopalan, Vicki H Wysocki
Published in
Analytica chimica acta. Volume 1426. Pages 346322. Dec 08, 2026. Epub Sep 24, 2026.
Abstract
Native mass spectrometry (nMS) and ion mobility (IM) are now established tools for the structural analysis of proteins and protein complexes, but their application to RNAs and RNA-RNA assemblies remains less developed. Here, we examine how magnesium, ionization polarity, solution temperature, and collisional activation influence the mass-corrected collision cross section (mCCS) of wild-type (WT) and a structurally destabilized mutant (MT) yeast tRNAPhe. Under positive-polarity ionization, magnesium was essential for WT tRNAPhe to fold into and retain native-like structures. In 2 mM magnesium acetate, increasing the solution temperature from 25 to 60°C produced little change in the mCCS of WT tRNAPhe, whereas the mCCS of MT tRNAPhe increased. Collisional activation further distinguished the two constructs: increasing the trap collision energy induced a pronounced decrease in the mCCS of WT but only a modest decrease for MT tRNAPhe, consistent with the absence of magnesium-supported tertiary contacts in the mutant. We also assessed the HJ3 RNA-RNA heterodimer using collision- and surface-induced dissociation (CID and SID, respectively). CID primarily resulted in charge stripping, while SID generated proportionally charged monomers, indicating preservation of native quaternary contacts. Collectively, these results demonstrate how IM-nMS measurements can be leveraged to gain insights into the tertiary and quaternary RNA structures and their gas-phase stability.
PMID:
42967776
Bibliographic data and abstract were imported from PubMed on 02 Nov 2026.
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