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
, 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

Department of Physics - at Bar-Ilan University

Indiana University Bloomington
NSWC Crane Division
University of California at Berkeley
Texas A&M University

Research output: Contribution to journal › Article › peer-review

24 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 language	English
Pages (from-to)	3270-3273
Number of pages	4
Journal	Chemical Communications
Volume	54
Issue number	26
DOIs	https://doi.org/10.1039/c7cc09829d
State	Published - 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.

Funders	Funder number
Robert and Marjorie Mann endowment
Waters Corporation
National Institutes of Health	R01 GM121751-01A1
National Institute of General Medical Sciences	R01GM117207
Indiana University

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10.1039/c7cc09829d

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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.",

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

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AU - El-Baba, Tarick J.

AU - Fuller, Daniel R.

AU - Woodall, Daniel W.

AU - Raab, Shannon A.

AU - Conant, Christopher R.

AU - Dilger, Jonathan M.

AU - Toker, Yoni

AU - Williams, Evan R.

AU - Russell, David H.

AU - Clemmer, David E.

PY - 2018/3/27

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AB - 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.

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JO - Chemical Communications

JF - Chemical Communications

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

Abstract

Bibliographical note

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