Melting proteins confined in nanodroplets with 10.6 μm light provides clues about early steps of denaturation

Tarick J. El-Baba, Daniel R. Fuller, Daniel W. Woodall, Shannon A. Raab, Christopher R. Conant, Jonathan M. Dilger, Yoni Toker, Evan R. Williams, David H. Russell, David E. Clemmer

Research output: Contribution to journalArticlepeer-review

21 Scopus citations

Abstract

Ubiquitin confined within nanodroplets was irradiated with a variable-power CO2 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.

Original languageEnglish
Pages (from-to)3270-3273
Number of pages4
JournalChemical Communications
Volume54
Issue number26
DOIs
StatePublished - 27 Mar 2018

Bibliographical note

Publisher Copyright:
© 2018 The Royal Society of Chemistry.

Funding

This work is supported in part by funds from the Waters Corporation, the National Institutes of Health R01 GM117207-03 and R01 GM121751-01A1, and the Robert and Marjorie Mann endowment. T. J. E. was supported by the Robert and Marjorie Mann fellowship from Indiana University.

FundersFunder number
Robert and Marjorie Mann endowment
Waters Corporation
National Institutes of HealthR01 GM121751-01A1
National Institute of General Medical SciencesR01GM117207
Indiana University

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