ArticleThe Journal of biological chemistry2019
Dynamic ion pair behavior stabilizes single α-helices in proteins.
Article in The Journal of biological chemistry, 2019. 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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Who cites it
11 citing papers in PubMed.
- Investigation of salt-bridge interactions underlying salt activation of halophilic methionine sulfoxide reductase A.Frontiers in microbiology · 2026Article
- Insight into improved specificity and thermostability of3 Biotech · 2025Article
- Dynamic Interchange of Local Residue-Residue Interactions in the Largely Extended Single Alpha-Helix in Drebrin.The Biochemical journal · 2025Article
- Article
- Inhibition of Aurora-A/N-Myc Protein-Protein Interaction Using Peptidomimetics: Understanding the Role of Peptide Cyclization.Chembiochem : a European journal of chemical biology · 2024Article
- Article
- Generalized Born Implicit Solvent Models Do Not Reproduce Secondary Structures ofJournal of chemical theory and computation · 2022Article
- α-Helix stabilization by co-operative side chain charge-reinforced interactions to phosphoserine in a basic kinase-substrate motif.The Biochemical journal · 2022Article
- ER/K-link-Leveraging a native protein linker to probe dynamic cellular interactions.Methods in enzymology · 2021Review
- Modulating the Stiffness of the Myosin VI Single α-Helical Domain.Biophysical journal · 2020Article
- Remarkable Rigidity of the Single α-Helical Domain of Myosin-VI As Revealed by NMR Spectroscopy.Journal of the American Chemical Society · 2019Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Ion pairs are key stabilizing interactions between oppositely charged amino acid side chains in proteins. They are often depicted as single conformer salt bridges (hydrogen-bonded ion pairs) in crystal structures, but it is unclear how dynamic they are in solution. Ion pairs are thought to be particularly important in stabilizing single α-helix (SAH) domains in solution. These highly stable domains are rich in charged residues (such as Arg, Lys, and Glu) with potential ion pairs across adjacent turns of the helix. They provide a good model system to investigate how ion pairs can contribute to protein stability. Using NMR spectroscopy, small-angle X-ray light scattering (SAXS), and molecular dynamics simulations, we provide here experimental evidence that ion pairs exist in a SAH in murine myosin 7a (residues 858-935), but that they are not fixed or long lasting.
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Registered trials
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