ArticleProtein science : a publication of the Protein Society2011
Modulating repeat protein stability: the effect of individual helix stability on the collective behavior of the ensemble.
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 17 papers.
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Who cites it
17 citing papers in PubMed.
- Engineered Protein-Based Ionic Conductors for Sustainable Energy Storage Applications.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- Engineered Protein-Driven Synthesis of Tunable Iron Oxide Nanoparticles as T1 and T2 Magnetic Resonance Imaging Contrast Agents.Chemistry of materials : a publication of the American Chemical Society · 2022Article
- Unraveling the Mechanics of a Repeat-Protein Nanospring: From Folding of Individual Repeats to Fluctuations of the Superhelix.ACS nano · 2022Article
- Engineered Repeat Protein Hybrids: The New Horizon for Biologic Medicines and Diagnostic Tools.Accounts of chemical research · 2021Article
- Engineering mono- and multi-valent inhibitors on a modular scaffold.Chemical science · 2021Article
- A collection of programs for one-dimensional Ising analysis of linear repeat proteins with point substitutions.Protein science : a publication of the Protein Society · 2021Article
- Engineering multifunctional metal/protein hybrid nanomaterials as tools for therapeutic intervention and high-sensitivity detection.Chemical science · 2020Article
- Engineered protein-based functional nanopatterned materials for bio-optical devices.Nanoscale advances · 2019Article
- Exploring new strategies for grafting binding peptides onto protein loops using a consensus-designed tetratricopeptide repeat scaffold.Protein science : a publication of the Protein Society · 2019Article
- Sensors Based on Metal Nanoclusters Stabilized on Designed Proteins.Biosensors · 2018Article
- Folding cooperativity and allosteric function in the tandem-repeat protein class.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- Removal of a consensus proline is not sufficient to allow tetratricopeptide repeat oligomerization.Protein science : a publication of the Protein Society · 2017Article
- Repeat protein scaffolds: ordering photo- and electroactive molecules in solution and solid state.Chemical science · 2016Article
- A designed repeat protein as an affinity capture reagent.Biochemical Society transactions · 2015Review
- General mechanism of two-state protein folding kinetics.Journal of the American Chemical Society · 2014Article
- Nanostructured functional films from engineered repeat proteins.Journal of the Royal Society, Interface · 2013Article
- Designed ankyrin repeat proteins as scaffolds for multivalent recognition.Biomacromolecules · 2012Article
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3 authors.
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Abstract
Repeat proteins are tandem arrays of a small structural motif, in which tertiary structure is stabilized by interactions within a repeat and between neighboring repeats. Several studies have shown that this modular structure is manifest in modular thermodynamic properties. Specifically, the global stability of a repeat protein can be described by simple linear models, considering only two parameters: the stability of the individual repeated units (H) and the coupling interaction between the units (J). If the repeat units are identical, single values of H and J, together with the number of repeated units, is sufficient to completely describe the thermodynamic behavior of any protein within a series. In this work, we demonstrate how the global stability of a repeat protein can be changed, in a predictable fashion, by modifying only the H parameter. Taking a previously characterized series of consensus tetratricopeptide repeats (TPR) (CTPRa) proteins, we introduced mutations into the basic repeating unit, such that the stability of the individual repeat unit was increased, but its interaction with neighboring units was unchanged. In other words, we increased H but kept J constant. We demonstrated that the denaturation curves for a series of such repeat proteins can be fit and additional curves can be predicted by the one-dimensional Ising model in which only H has changed from the original fit for the CTPRa series. Our results show that we can significantly increase the stability of a repeat protein by rationally increasing the stability of the units (H), whereas the interaction between repeats (J) remains unchanged.
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