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Native Biomolecules in the Gas Phase? The Case of Green Fluorescent Protein
Author(s) -
Frankevich Vladimir,
Barylyuk Konstantin,
Chingin Konstantin,
Nieckarz Robert,
Zenobi Renato
Publication year - 2013
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.201200959
Subject(s) - green fluorescent protein , fluorescence , chromophore , chemistry , biomolecule , gas phase , dissociation (chemistry) , mass spectrometry , photochemistry , electrospray ionization , ionization , analytical chemistry (journal) , ion , chromatography , organic chemistry , biochemistry , physics , gene , quantum mechanics
Green fluorescent protein (GFP) was ionized by native electrospray ionization and trapped for many seconds in high vacuum, allowing fluorescence emission to be measured as a probe of its biological function, to answer the question whether GFP exists in the native form in the gas phase or not. Although a narrow charge‐state distribution, a collision cross‐section very close to that expected for correctly folded GFP, and a large stability against dissociation all support a near‐native gas‐phase structure, no fluorescence emission was observed. The loss of the native form is attributed to the absence of residual water in the gas phase, which normally stabilizes the para ‐hydroxybenzylidene imidazolone chromophore of GFP.