ArticleJournal of the American Chemical Society2019
Remarkable Rigidity of the Single α-Helical Domain of Myosin-VI As Revealed by NMR Spectroscopy.
Article in Journal of the American Chemical Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Cryo-EM structure of ALC1 in an open conformation bound to a PARylated nucleosome.Acta crystallographica. Section D, Structural biology · 2026Article
- Two-conformer equilibrium of maltose-binding protein in the absence of ligand from residual dipolar coupling analysis.Protein science : a publication of the Protein Society · 2026Article
- Dynamic Interchange of Local Residue-Residue Interactions in the Largely Extended Single Alpha-Helix in Drebrin.The Biochemical journal · 2025Article
- ER-mitochondria distance is a critical parameter for efficient mitochondrial CaCommunications biology · 2024Article
- Engineering Agonistic Bispecifics to Investigate the Influence of Distance on Surface-Mediated Complement Activation.Journal of immunology (Baltimore, Md. : 1950) · 2024Article
- Conformations of a highly expressed Z19 α-zein studied with AlphaFold2 and MD simulations.PloS one · 2024Article
- Tad and toxin-coregulated pilus structures reveal unexpected diversity in bacterial type IV pili.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Systematic identification of conditionally folded intrinsically disordered regions by AlphaFold2.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- How myosin VI traps its off-state, is activated and dimerizes.Nature communications · 2023Article
- Article
- Magnetic control of self-assembly and disassembly in organic materials.Nature communications · 2023Article
- Uncovering the Contributions of Charge Regulation to the Stability of Single Alpha Helices.Chemphyschem : a European journal of chemical physics and physical chemistry · 2023Article
- Engineering the Active Site Lid Dynamics to Improve the Catalytic Efficiency of Yeast Cytosine Deaminase.International journal of molecular sciences · 2023Article
- A structural model of the profilin-formin pacemaker system for actin filament elongation.Scientific reports · 2022Article
- Landscape-Based View on the Stepping Movement of Myosin VI.The journal of physical chemistry. B · 2022Article
- Paramagnetic Chemical Probes for Studying Biological Macromolecules.Chemical reviews · 2022Review
- High-Resolution Hydrogen-Deuterium Protection Factors from Sparse Mass Spectrometry Data Validated by Nuclear Magnetic Resonance Measurements.Journal of the American Society for Mass Spectrometry · 2022Article
- DIPEND: An Open-Source Pipeline to Generate Ensembles of Disordered Segments Using Neighbor-Dependent Backbone Preferences.Biomolecules · 2021Article
- Four-dimensional NOE-NOE spectroscopy of SARS-CoV-2 Main Protease to facilitate resonance assignment and structural analysis.Magnetic resonance (Gottingen, Germany) · 2021Article
- Detecting anisotropic segmental dynamics in disordered proteins by cross-correlated spin relaxation.Magnetic resonance (Gottingen, Germany) · 2021Article
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7 authors.
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Abstract
Although the α-helix has long been recognized as an all-important element of secondary structure, it generally requires stabilization by tertiary interactions with other parts of a protein's structure. Highly charged single α-helical (SAH) domains, consisting of a high percentage (>75%) of Arg, Lys, and Glu residues, are exceptions to this rule but have been difficult to characterize structurally. Our study focuses on the 68-residue medial tail domain of myosin-VI, which is found to contain a highly ordered α-helical structure extending from Glu-6 to Lys-63. High hydrogen exchange protection factors (15-150), small (ca. 4 Hz)
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