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

Bar-Ilan University

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

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

All Science Journal Classification (ASJC) codes

Electronic, Optical and Magnetic Materials
Catalysis
Ceramics and Composites
General Chemistry
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

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10.1039/c7cc09829d

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

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.\}",

note = "Publisher Copyright: {\textcopyright} 2018 The Royal Society of Chemistry.",

year = "2018",

month = mar,

day = "27",

doi = "10.1039/c7cc09829d",

language = "الإنجليزيّة",

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TY - JOUR

T1 - Melting proteins confined in nanodroplets with 10.6 μm light provides clues about early steps of denaturation

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

Y1 - 2018/3/27

N2 - 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.

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.

UR - http://www.scopus.com/inward/record.url?scp=85044677573&partnerID=8YFLogxK

U2 - 10.1039/c7cc09829d

DO - 10.1039/c7cc09829d

M3 - مقالة

C2 - 29536995

SN - 1359-7345

VL - 54

SP - 3270

EP - 3273

JO - Chemical Communications

JF - Chemical Communications

IS - 26

ER -

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

Abstract

All Science Journal Classification (ASJC) codes

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