Conformational landscapes of rigid and flexible molecules explored with variable temperature ion mobility-mass spectrometry
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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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Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works
α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation
Bartels, T., Choi, J. G., & Selkoe, D. J. (2011) · Nature · doi:10.1038/nature10324 · Cited by 1,263 · cited 1× · see citing works
“It has been suggested that α -synuclein may form a more stable helical structure in a highly hydrophobic environment 63,66,67 .”
Native mass spectrometry: a bridge between interactomics and structural biology
Heck, A. J. R. (2008) · Nature Methods · doi:10.1038/nmeth.1265 · Cited by 766 · see citing works
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- Authors
- Wang, X., Norgate, E., Dai, J., Benoit, F., Bristow, T., England, R. M., Kalapothakis, J. M. D., & Barran, P. E.
- Affiliations
- University of Manchester (GB)
- AstraZeneca (United Kingdom) (GB)
- Corresponding author
- Barran, Perdita E.
- Venue
- Nature Communications
- Published
- 2025-05-06
- Volume
- 16
- Issue
- 1
- Pages
- 4183-4183
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC12052783
- OpenAlex
- W4410082400
- Cited by
- 7
- References
- 3
- Citations by year
- 2026: 5 · 2025: 2
- FWCI
- 1.77
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- ChemRxiv (acceptedVersion, cc-by-nc-nd)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Research Explorer (The University of Manchester) (submittedVersion)
- Funders
- RCUK | Engineering and Physical Sciences Research Council (EP/T019328/1, EP/S005226/1)
- RCUK | Biotechnology and Biological Sciences Research Council (BB/X003027/1)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Keywords
- conformational landscape, protein thermal stability, ubiquitin, β-casein, alpha-synuclein, collision-induced dissociation, unfolding intermediates, activation energy
- MeSH terms
- Ion Mobility Spectrometry, Caseins, Kinetics, Polylysine, Protein Conformation, Mass Spectrometry, Temperature, Thermodynamics, Ubiquitin, Dendrimers, alpha-Synuclein
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