ArticleNature communications2025
Conformational landscapes of rigid and flexible molecules explored with variable temperature ion mobility-mass spectrometry.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- Hyphenated Mass Spectrometry-Based Strategies for Characterizing Oligomers of α‑Synuclein in Parkinson's Disease.ACS central science · 2026Article
- Multifunctional nanoplatforms deciphering immune resistance in bone tumors: cooperative delivery, immune reprogramming and microenvironment remodeling.Journal of nanobiotechnology · 2026Review
- Drug screening for α-synuclein aggregation inhibitors via multimodal graph neural network.Briefings in bioinformatics · 2026Article
- Study on the astringent mechanism ofFood chemistry: X · 2025Article
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Authors and funding
8 authors.
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Abstract
Understanding the effect of temperature to the structural integrity of proteins is relevant to diverse areas such as biotechnology and climate change. Variable temperature ion mobility-mass spectrometry (VT-IM-MS) can measure the effect of temperature on conformational landscapes. To delineate collision effects from structural change we report measurements using molecules with different degrees of rigidity namely: poly (L-lysine) (PLL) dendrimer, ubiquitin, β-casein and α-synuclein from 190-350 K. The CCS of PLL dendrimer varies with temperature consistent with collision theory, by contrast, the structure of each protein alters with notable restructuring at 350 K and 250 K, following predicted in vitro stability curves. At 210 K and 190 K we kinetically trap unfolding intermediates. For alpha-synuclein, the 13+ ions present two distinct conformers and VT-IM-MS measurements allow us to calculate the transition rate and activation energies of their conversion. These data exemplify the capacity of VT-IM-MS to provide insights on the thermodynamics of conformational restructuring.
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