ArticleFrontiers in molecular biosciences2014
Trapping a salt-dependent unfolding intermediate of the marginally stable protein Yfh1.
Article in Frontiers in molecular biosciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Heat and cold denaturation of yeast frataxin: The effect of pressure.Biophysical journal · 2022Article
- The anatomy of unfolding of Yfh1 is revealed by site-specific fold stability analysis measured by 2D NMR spectroscopy.Communications chemistry · 2021Article
- Quantifying the thermodynamics of protein unfolding using 2D NMR spectroscopy.Communications chemistry · 2020Article
- The role of oxidative stress in Friedreich's ataxia.FEBS letters · 2018Review
- Human Frataxin Folds Via an Intermediate State. Role of the C-Terminal Region.Scientific reports · 2016Article
- Selective observation of the disordered import signal of a globular protein by in-cell NMR: the example of frataxins.Protein science : a publication of the Protein Society · 2015Article
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5 authors.
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Abstract
Yfh1, the yeast ortholog of frataxin, is a protein of limited thermodynamic stability which undergoes cold denaturation at temperatures above the water freezing point. We have previously demonstrated that its stability is strongly dependent on ionic strength and that monovalent or divalent cations are able to considerably stabilize the fold. Here, we present a study of the folded state and of the structural determinants that lead to the strong salt dependence. We demonstrate by nuclear magnetic resonance that, at room temperature, Yfh1 exists as an equilibrium mixture of a folded species and a folding intermediate in slow exchange equilibrium. The equilibrium completely shifts in favor of the folded species by the addition of even small concentrations of salt. We demonstrate that Yfh1 is destabilized by a localized energetic frustration arising from an "electrostatic hinge" made of negatively charged residues mapped in the β-sheet. Salt interactions at this site have a "frustration-relieving" effect. We discuss the consequences of our findings for the function of Yfh1 and for our understanding of protein folding stability.
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