ArticleProceedings of the National Academy of Sciences of the United States of America2019
Application of millisecond time-resolved solid state NMR to the kinetics and mechanism of melittin self-assembly.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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36 citing papers in PubMed, 76 citations in OpenAlex.
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- Time-resolved solid-state nuclear magnetic resonance studies of amyloid-β oligomer formation.Methods in enzymology · 2026Review
- Effects of Nanopore Confinement on the Conformational, Dynamical, and Self-Assembly Properties of an FG-Repeat Peptide.The journal of physical chemistry. B · 2025Article
- Effects of Nanopore Confinement on the Conformational, Dynamical, and Self-Assembly Properties of an FG-Repeat Peptide.bioRxiv : the preprint server for biology · 2025Article
- Quantification of Rapid Cooling of Glycerol/Water Solutions Based on Photoluminescence from Thioflavin T.The journal of physical chemistry. B · 2024Article
- Conformations of a low-complexity protein in homogeneous and phase-separated frozen solutions.Biophysical journal · 2024Article
- Optimization ofJournal of magnetic resonance (San Diego, Calif. : 1997) · 2024Article
- Conformations of a Low-Complexity Protein in Homogeneous and Phase-Separated Frozen Solutions.bioRxiv : the preprint server for biology · 2024Article
- Dynamic Nuclear Polarization Enhanced Multiple-Quantum Spin Counting of Molecular Assemblies in Vitrified Solutions.The journal of physical chemistry letters · 2024Article
- Real-Time Monitoring of Photoinduced pH Jumps byThe journal of physical chemistry letters · 2024Article
- From Milliseconds to Minutes: Melittin Self-Assembly from Concerted Non-Equilibrium Pressure-Jump and Equilibrium Relaxation Nuclear Magnetic Resonance.The journal of physical chemistry letters · 2024Article
- Experimental Evidence for Millisecond-Timescale Structural Evolution Following the Microsecond-Timescale Folding of a Small Protein.Physical review letters · 2024Article
- Dimerization and lysine substitution of melittin have differing effects on bacteria.Frontiers in pharmacology · 2024Article
- Early events in amyloid-β self-assembly probed by time-resolved solid state NMR and light scattering.Nature communications · 2023Article
- Spin Hyperpolarization in Modern Magnetic Resonance.Chemical reviews · 2023Review
- Characterization of conformational heterogeneity via higher-dimensionality, proton-detected solid-state NMR.Journal of biomolecular NMR · 2022Article
- Time-resolved solid state NMR of biomolecular processes with millisecond time resolution.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2022Review
- Nitroxide-based triradical dopants for efficient low-temperature dynamic nuclear polarization in aqueous solutions over a broad pH range.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2022Article
- Quantitative Agreement between Conformational Substates of Holo Calcium-Loaded Calmodulin Detected by Double Electron-Electron Resonance EPR and Predicted by Molecular Dynamics Simulations.Journal of the American Chemical Society · 2022Article
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Authors and funding
5 authors at 2 institutions in 1 country.
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Abstract
Common experimental approaches for characterizing structural conversion processes such as protein folding and self-assembly do not report on all aspects of the evolution from an initial state to the final state. Here, we demonstrate an approach that is based on rapid mixing, freeze-trapping, and low-temperature solid-state NMR (ssNMR) with signal enhancements from dynamic nuclear polarization (DNP). Experiments on the folding and tetramerization of the 26-residue peptide melittin following a rapid pH jump show that multiple aspects of molecular structure can be followed with millisecond time resolution, including secondary structure at specific isotopically labeled sites, intramolecular and intermolecular contacts between specific pairs of labeled residues, and overall structural order. DNP-enhanced ssNMR data reveal that conversion of conformationally disordered melittin monomers at low pH to α-helical conformations at neutral pH occurs on nearly the same timescale as formation of antiparallel melittin dimers, about 6 to 9 ms for 0.3 mM melittin at 24 °C in aqueous solution containing 20% (vol/vol) glycerol and 75 mM sodium phosphate. Although stopped-flow fluorescence data suggest that melittin tetramers form quickly after dimerization, ssNMR spectra show that full structural order within melittin tetramers develops more slowly, in ∼60 ms. Time-resolved ssNMR is likely to find many applications to biomolecular structural conversion processes, including early stages of amyloid formation, viral capsid formation, and protein-protein recognition.
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