ArticleBiophysical journal2005
Tracking unfolding and refolding of single GFPmut2 molecules.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Random single amino acid deletion sampling unveils structural tolerance and the benefits of helical registry shift on GFP folding and structure.Structure (London, England : 1993) · 2014Article
- Structural basis of fluorescence quenching in caspase activatable-GFP.Protein science : a publication of the Protein Society · 2013Article
- The shape-shifting quasispecies of RNA: one sequence, many functional folds.Physical chemistry chemical physics : PCCP · 2011Article
- Development of free-energy-based models for chaperonin containing TCP-1 mediated folding of actin.Journal of the Royal Society, Interface · 2008Review
- The rough energy landscape of superfolder GFP is linked to the chromophore.Journal of molecular biology · 2007Article
- Environment effects on the oscillatory unfolding kinetics of GFP.European biophysics journal : EBJ · 2007Article
- GFP-mut2 proteins in trehalose-water matrixes: spatially heterogeneous protein-water-sugar structures.Biophysical journal · 2007Article
- Evidence of discrete substates and unfolding pathways in green fluorescent protein.Biophysical journal · 2007Article
- Unfolding time distribution of GFP by single molecule fluorescence spectroscopy.European biophysics journal : EBJ · 2006Article
- Molecular fluorescence, phosphorescence, and chemiluminescence spectrometry.Analytical chemistry · 2006Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The unfolding and refolding kinetics of >600 single GFPmut2 molecules, entrapped in wet nanoporous silica gels, were followed by monitoring simultaneously the fluorescence emission of the anionic and neutral state of the chromophore, primed by two-photon excitation. The rate of unfolding, induced by guanidinium chloride, was determined by counting the number of single molecules that disappear in fluorescence images, under conditions that do not cause bleaching or photoinduced conversion between chromophore protonation states. The unfolding rate is of the order of 0.01 min(-1), and its dependence on denaturant concentration is very similar to that previously reported for high protein load gels. Upon rinsing the gels with denaturant-free buffer, the GFPmut2 molecules refold with rates >10 min(-1), with an apparently random distribution between neutral and anionic states, that can be very different from the preunfolding equilibrium. A subsequent very slow (lifetime of approximately 70 min) relaxation leads to the equilibrium distribution of the protonation states. This mechanism, involving one or more native-like refolding intermediates, is likely rate limited by conformational rearrangements that are undetectable in circular dichroism experiments. Several unfolding/refolding cycles can be followed on the same molecules, indicating full reversibility of the process and, noticeably, a bias of denaturated molecules toward refolding in the original protonation state.
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