| Literature DB >> 23436608 |
Vladimir Frankevich1, Konstantin Barylyuk, Konstantin Chingin, Robert Nieckarz, Renato Zenobi.
Abstract
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.Entities:
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Year: 2013 PMID: 23436608 DOI: 10.1002/cphc.201200959
Source DB: PubMed Journal: Chemphyschem ISSN: 1439-4235 Impact factor: 3.102