In:
ChemPhysChem, Wiley, Vol. 14, No. 5 ( 2013-04-02), p. 929-935
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.
Type of Medium:
Online Resource
ISSN:
1439-4235
,
1439-7641
DOI:
10.1002/cphc.201200959
Language:
English
Publisher:
Wiley
Publication Date:
2013
detail.hit.zdb_id:
2025223-7
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