ArticleScientific reports2016
Human Frataxin Folds Via an Intermediate State. Role of the C-Terminal Region.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 25 citations in OpenAlex.
- Frataxin: from the sequence to the biological role.Biophysical reviews · 2025Review
- Fifty years of biophysics in Argentina.Biophysical reviews · 2023Article
- Natural flavonoids effectively block the CD81 receptor of hepatocytes and inhibit HCV infection: a computational drug development approach.Molecular diversity · 2023Article
- Modelling Protein Plasticity: The Example of Frataxin and Its Variants.Molecules (Basel, Switzerland) · 2022Article
- Protein Mutations and Stability, a Link with Disease: The Case Study of Frataxin.Biomedicines · 2022Review
- Effects of FeInternational journal of molecular sciences · 2020Article
- A Highly Conserved Iron-Sulfur Cluster Assembly Machinery between Humans and AmoebaInternational journal of molecular sciences · 2020Article
- Evaluating the predictions of the protein stability change upon single amino acid substitutions for the FXN CAGI5 challenge.Human mutation · 2019Article
- Global Implications of Local Unfolding Phenomena, Probed by Cysteine Reactivity in Human Frataxin.Scientific reports · 2019Article
- PFDB: A standardized protein folding database with temperature correction.Scientific reports · 2019Article
- Biophysical characterisation of the recombinant human frataxin precursor.FEBS open bio · 2018Article
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Authors and funding
4 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The aim of this study is to investigate the folding reaction of human frataxin, whose deficiency causes the neurodegenerative disease Friedreich's Ataxia (FRDA). The characterization of different conformational states would provide knowledge about how frataxin can be stabilized without altering its functionality. Wild-type human frataxin and a set of mutants, including two highly destabilized FRDA-associated variants were studied by urea-induced folding/unfolding in a rapid mixing device and followed by circular dichroism. The analysis clearly indicates the existence of an intermediate state (I) in the folding route with significant secondary structure content but relatively low compactness, compared with the native ensemble. However, at high NaCl concentrations I-state gains substantial compaction, and the unfolding barrier is strongly affected, revealing the importance of electrostatics in the folding mechanism. The role of the C-terminal region (CTR), the key determinant of frataxin stability, was also studied. Simulations consistently with experiments revealed that this stretch is essentially unstructured, in the most compact transition state ensemble (TSE2). The complete truncation of the CTR drastically destabilizes the native state without altering TSE2. Results presented here shed light on the folding mechanism of frataxin, opening the possibility of mutating it to generate hyperstable variants without altering their folding kinetics.
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