title: Native biomolecules in the gas phase? The case of green fluorescent protein.
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.
authors: Department of Chemistry and Applied Biosciences, ETH Zürich, Zürich, Switzerland.
authors: Vladimir
authors: V
authors: Frankevich
authors: Konstantin
authors: K
authors: Barylyuk
authors: Konstantin
authors: K
authors: Chingin
authors: Robert
authors: R
authors: Nieckarz
authors: Renato
authors: R
authors: Zenobi
mesh_terms: D005453:Fluorescence; D005456:Fluorescent Dyes / Q000737:chemistry*; D005740:Gases / Q000737:chemistry*; D049452:Green Fluorescent Proteins / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D011994:Recombinant Proteins / Q000737:chemistry; D021241:Spectrometry, Mass, Electrospray Ionization; D014618:Vacuum; D014867:Water / Q000737:chemistry
chemical_list: D005456:Fluorescent Dyes; D005740:Gases; D011994:Recombinant Proteins; D014867:Water; D049452:Green Fluorescent Proteins