ArticleEuropean biophysics journal : EBJ2006
Unfolding time distribution of GFP by single molecule fluorescence spectroscopy.
Article in European biophysics journal : EBJ, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Beta-barrel scaffold of fluorescent proteins: folding, stability and role in chromophore formation.International review of cell and molecular biology · 2013Review
- Folding study of Venus reveals a strong ion dependence of its yellow fluorescence under mildly acidic conditions.The Journal of biological chemistry · 2010Article
- Raman Tweezers as a Diagnostic Tool of Hemoglobin-Related Blood Disorders.Sensors (Basel, Switzerland) · 2008Review
- Environment effects on the oscillatory unfolding kinetics of GFP.European biophysics journal : EBJ · 2007Article
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Authors and funding
3 authors.
Funding
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Abstract
We have studied the unfolding of single molecules of GFP-mut2 mutant trapped in wet silica gels in a wide range of GuHCl concentration. After the addition of denaturant, the number of fluorescent molecules decreases with unfolding rates (of the order of 0.01 min(-1)) that are in very good agreement with bulk fluorescence and circular dichroism data. Unexpectedly, single molecule experiments show rare fluctuations in the number of fluorescent proteins at equilibrium. On the other hand, although a first approximate description of the number decays can be reasonably performed by single exponential functions, the distributions of the single molecule unfolding times show a maximum at times congruent with 50-100 min up to the denaturation midpoint concentration of [GuHCl] congruent with 2.5 M. A theoretical analysis of the distributions indicates that this feature is a fingerprint of the competition between unfolding and refolding processes when the protein is very far from the midpoint denaturant concentration.
Indexed as
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Registered trials
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