Melting proteins confined in nanodroplets with 10.6 $\mu$m light provides clues about early steps of denaturation

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dc.contributor.authorEl-Baba, T J
dc.contributor.authorFuller, D R
dc.contributor.authorWoodall, D W
dc.contributor.authorRaab, S A
dc.contributor.authorConant, C R
dc.contributor.authorDilger, J M
dc.contributor.authorToker, Y
dc.contributor.authorWilliams, E R
dc.contributor.authorRussell, D H
dc.contributor.authorClemmer, David E.
dc.date.accessioned2025-02-20T15:49:52Z
dc.date.available2025-02-20T15:49:52Z
dc.date.issued2019-03-27
dc.description.abstractUbiquitin confined within nanodroplets was irradiated with a variable-power CO$_2$ laser. Mass spectrometry analysis shows evidence for a protein “melting”-like transition within droplets prior to solvent evaporation and ion formation. Ion mobility spectrometry reveals that structures associated with early steps of denaturation are trapped because of short droplet lifetimes.
dc.identifier.citationEl-Baba, T J, et al. "Melting proteins confined in nanodroplets with 10.6 $\mu$m light provides clues about early steps of denaturation." Chemical Communications, vol. 54, no. 26, pp. 3270-3273, 2019-03-27, https://doi.org/10.1039/c7cc09829d.
dc.identifier.otherBRITE 2016
dc.identifier.urihttps://hdl.handle.net/2022/30825
dc.language.isoen
dc.relation.isversionofhttps://doi.org/10.1039/c7cc09829d
dc.relation.isversionofhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5871606
dc.relation.journalChemical Communications
dc.titleMelting proteins confined in nanodroplets with 10.6 $\mu$m light provides clues about early steps of denaturation

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