Literature DB >> 23436608

Native biomolecules in the gas phase? The case of green fluorescent protein.

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.
Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

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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


  2 in total

1.  Gas-phase protein conformation/multimer ion formation by electrospray ion mobility-mass spectrometry: bovine insulin and ubiquitin.

Authors:  Kent J Gillig
Journal:  Philos Trans A Math Phys Eng Sci       Date:  2016-10-28       Impact factor: 4.226

2.  Proteins with highly similar native folds can show vastly dissimilar folding behavior when desolvated.

Authors:  Moritz Schennach; Kathrin Breuker
Journal:  Angew Chem Int Ed Engl       Date:  2013-11-20       Impact factor: 15.336

  2 in total

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