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

doi:10.1039/C7CC09829D

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

Tarick J. El-Baba,^a Daniel R. Fuller,^a Daniel W. Woodall,^a Shannon A. Raab,^a Christopher R. Conant,^a Jonathan M. Dilger,

^b Yoni Toker,^c Evan R. Williams,

^d David H. Russell

^e and David E. Clemmer

*^a

Author affiliations

* Corresponding authors

^a Department of Chemistry, Indiana University, 800 Kirkwood Avenue, Bloomington, 47401, Indiana, USA
E-mail: clemmer@indiana.edu

^b Spectrum Warfare Systems Department, NSWC Crane Division, Crane, Indiana, USA

^c Department of Physics and Inst. of Nanotechnology, Bar-Ilan University, Ramat-Gan 5290002, Israel

^d Department of Chemistry, University of California, Berkeley, California, USA

^e Department of Chemistry, Texas A&M University, College Station, Texas, USA

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.

Chemical Communications

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

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

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