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Melting proteins confined in nanodroplets with 10.6 ?m 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.

SUBMITTER: El-Baba TJ 

PROVIDER: S-EPMC5871606 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature

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

El-Baba Tarick J TJ   Fuller Daniel R DR   Woodall Daniel W DW   Raab Shannon A SA   Conant Christopher R CR   Dilger Jonathan M JM   Toker Yoni Y   Williams Evan R ER   Russell David H DH   Clemmer David E DE  

Chemical communications (Cambridge, England) 20180301 26


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. ...[more]

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