ArticleProtein science : a publication of the Protein Society2011
Calorimetric study of a series of designed repeat proteins: modular structure and modular folding.
Article in Protein science : a publication of the Protein Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- pH-Dependent Stability and Cooperativity of Protein Unfolding from Differential Scanning Calorimetry Using FitFoldData.Biomolecules · 2026Article
- Unraveling the Mechanics of a Repeat-Protein Nanospring: From Folding of Individual Repeats to Fluctuations of the Superhelix.ACS nano · 2022Article
- Engineered protein-based functional nanopatterned materials for bio-optical devices.Nanoscale advances · 2019Article
- Ambidextrous helical nanotubes from self-assembly of designed helical hairpin motifs.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Sensors Based on Metal Nanoclusters Stabilized on Designed Proteins.Biosensors · 2018Article
- Protein knotting through concatenation significantly reduces folding stability.Scientific reports · 2016Article
- Repeat protein scaffolds: ordering photo- and electroactive molecules in solution and solid state.Chemical science · 2016Article
- Evolution under Drug Pressure Remodels the Folding Free-Energy Landscape of Mature HIV-1 Protease.Journal of molecular biology · 2016Article
- Ising Model Reprogramming of a Repeat Protein's Equilibrium Unfolding Pathway.Journal of molecular biology · 2016Article
- Article
- A Naturally Occurring Repeat Protein with High Internal Sequence Identity Defines a New Class of TPR-like Proteins.Structure (London, England : 1993) · 2015Article
- The unexpected role of polyubiquitin chains in the formation of fibrillar aggregates.Nature communications · 2015Article
- Intermediates in the folding equilibrium of repeat proteins from the TPR family.European biophysics journal : EBJ · 2014Article
- Article
- Modulation of the multistate folding of designed TPR proteins through intrinsic and extrinsic factors.Protein science : a publication of the Protein Society · 2012Article
- Modulating repeat protein stability: the effect of individual helix stability on the collective behavior of the ensemble.Protein science : a publication of the Protein Society · 2011Article
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2 authors.
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Abstract
Repeat proteins comprise tandem arrays of a small structural motif. Their structure is defined and stabilized by interactions between residues that are close in the primary sequence. Several studies have investigated whether their structural modularity translates into modular thermodynamic properties. Tetratricopeptide repeat proteins (TPRs) are a class in which the repeated unit is a 34 amino acid helix-turn-helix motif. In this work, we use differential scanning calorimetry (DSC) to study the equilibrium stability of a series of TPR proteins with different numbers of an identical consensus repeat, from 2 to 20, CTPRa2 to CTPRa20. The DSC data provides direct evidence that the folding/unfolding transition of CTPR proteins does not fit a two-state folding model. Our results confirm and expand earlier studies on TPR proteins, which showed that apparent two-state unfolding curves are better fit by linear statistical mechanics models: 1D Ising models in which each repeat is treated as an independent folding unit.
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