ArticleProceedings of the National Academy of Sciences of the United States of America2008
Shifting transition states in the unfolding of a large ankyrin repeat protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Small Molecule Activators of Protein Phosphatase 2A Exert Global Stabilizing Effects on the Scaffold PR65.JACS Au · 2026Article
- Unraveling the Mechanics of a Repeat-Protein Nanospring: From Folding of Individual Repeats to Fluctuations of the Superhelix.ACS nano · 2022Article
- Resolving the fine structure in the energy landscapes of repeat proteins.QRB discovery · 2022Article
- Multivalent Interaction of Beta-Catenin With its Intrinsically Disordered Binding Partner Adenomatous Polyposis Coli.Frontiers in molecular biosciences · 2022Article
- Parallel and Sequential Pathways of Molecular Recognition of a Tandem-Repeat Protein and Its Intrinsically Disordered Binding Partner.Biomolecules · 2021Article
- Large Ankyrin repeat proteins are formed with similar and energetically favorable units.PloS one · 2020Article
- Decoupling a tandem-repeat protein: Impact of multiple loop insertions on a modular scaffold.Scientific reports · 2019Article
- Folding cooperativity and allosteric function in the tandem-repeat protein class.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- Disorder drives cooperative folding in a multidomain protein.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Structural and Energetic Characterization of the Ankyrin Repeat Protein Family.PLoS computational biology · 2015Article
- Even with nonnative interactions, the updated folding transition states of the homologs Proteins G & L are extensive and similar.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Single-molecule chemo-mechanical unfolding reveals multiple transition state barriers in a small single-domain protein.Nature communications · 2015Article
- Mutagenesis of Trichoderma reesei endoglucanase I: impact of expression host on activity and stability at elevated temperatures.BMC biotechnology · 2015Article
- Single-molecule FRET reveals hidden complexity in a protein energy landscape.Structure (London, England : 1993) · 2015Article
- Frustration in biomolecules.Quarterly reviews of biophysics · 2014Review
- Direct observation of parallel folding pathways revealed using a symmetric repeat protein system.Biophysical journal · 2014Article
- Complex energy landscape of a giant repeat protein.Structure (London, England : 1993) · 2013Article
- Mechanical anisotropy of ankyrin repeats.Biophysical journal · 2012Article
- Article
- Cytoplasmic ankyrin repeats of transient receptor potential A1 (TRPA1) dictate sensitivity to thermal and chemical stimuli.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
Corrections and comments
- Commented on by
- Erratum issued
Authors and funding
4 authors.
Funding
Abstract
The 33-amino-acid ankyrin motif comprises a beta-turn followed by two anti-parallel alpha-helices and a loop and tandem arrays of the motif pack in a linear fashion to produce elongated structures characterized by short-range interactions. In this article we use site-directed mutagenesis to investigate the kinetic unfolding mechanism of D34, a 426-residue, 12-ankyrin repeat fragment of the protein ankyrinR. The data are consistent with a model in which the N-terminal half of the protein unfolds first by unraveling progressively from the start of the polypeptide chain to form an intermediate; in the next step, the C-terminal half of the protein unfolds via two pathways whose transition states have either the early or the late C-terminal ankyrin repeats folded. We conclude that the two halves of the protein unfold by different mechanisms because the N-terminal moiety folds and unfolds in the context of a folded C-terminal moiety, which therefore acts as a "seed" and confers a unique directionality on the process, whereas the C-terminal moiety folds and unfolds in the context of an unfolded N-terminal moiety and therefore behaves like a single-domain ankyrin repeat protein, having a high degree of symmetry and consequently more than one unfolding pathway accessible to it.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.