ArticleThe Journal of biological chemistry2014
Stable single α-helices are constant force springs in proteins.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
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- Co-translational ribosome pairing enables native assembly of misfolding-prone subunits.Nature communications · 2025Article
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- Backbone Hydration ofMolecular physics · 2024Article
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- PK1 fromOpen biology · 2023Article
- Contribution of hydrophobic interactions to protein mechanical stability.Computational and structural biotechnology journal · 2022Article
- Switching an active site helix in dihydrofolate reductase reveals limits to subdomain modularity.Biophysical journal · 2021Article
- Titin kinase ubiquitination aligns autophagy receptors with mechanical signals in the sarcomere.EMBO reports · 2021Article
- When Familial Hearing Loss Means Genetic Heterogeneity: A Model Case Report.Diagnostics (Basel, Switzerland) · 2021Article
- ER/K-link-Leveraging a native protein linker to probe dynamic cellular interactions.Methods in enzymology · 2021Review
- Structure of the shutdown state of myosin-2.Nature · 2020Article
- Disentangling the complexity of low complexity proteins.Briefings in bioinformatics · 2020Review
- Modulating the Stiffness of the Myosin VI Single α-Helical Domain.Biophysical journal · 2020Article
- Single-Molecule Force Spectroscopy on the N2A Element of Titin: Effects of Phosphorylation and CARP.Frontiers in physiology · 2020Article
- Helix 8 is the essential structural motif of mechanosensitive GPCRs.Nature communications · 2019Article
- Probing the Basis of α-Synuclein Aggregation by Comparing Simulations to Single-Molecule Experiments.Biophysical journal · 2019Article
- Remarkable Rigidity of the Single α-Helical Domain of Myosin-VI As Revealed by NMR Spectroscopy.Journal of the American Chemical Society · 2019Article
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6 authors.
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Abstract
Single α-helix (SAH) domains are rich in charged residues (Arg, Lys, and Glu) and stable in solution over a wide range of pH and salt concentrations. They are found in many different proteins where they bridge two functional domains. To test the idea that their high stability might enable these proteins to resist unfolding along their length, the properties and unfolding behavior of the predicted SAH domain from myosin-10 were characterized. The expressed and purified SAH domain was highly helical, melted non-cooperatively, and was monomeric as shown by circular dichroism and mass spectrometry as expected for a SAH domain. Single molecule force spectroscopy experiments showed that the SAH domain unfolded at very low forces (<30 pN) without a characteristic unfolding peak. Molecular dynamics simulations showed that the SAH domain unfolds progressively as the length is increased and refolds progressively as the length is reduced. This enables the SAH domain to act as a constant force spring in the mechanically dynamic environment of the cell.
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