ArticleProceedings of the National Academy of Sciences of the United States of America2022
Time-resolved DEER EPR and solid-state NMR afford kinetic and structural elucidation of substrate binding to Ca
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 44 citations in OpenAlex.
- EPR spectroscopy 80 years after its discovery.Science advances · 2026Review
- Protocol for preparing and characterizing samples for combined microsecond freeze-hyperquenching and electron paramagnetic resonance spectroscopy.STAR protocols · 2026Article
- Direct observation and measurement of the average quantum methyl-tunneling frequency in a protein usingChemical communications (Cambridge, England) · 2026Article
- Time-resolved solid-state nuclear magnetic resonance studies of amyloid-β oligomer formation.Methods in enzymology · 2026Review
- A high-sensitivity stopped-flow EPR system to monitor millisecond conformational kinetics in spin-labeled proteins.Protein science : a publication of the Protein Society · 2025Article
- Capturing protein dynamics across timescales with site-directed spin labeling electron paramagnetic resonance spectroscopy.Current opinion in structural biology · 2025Review
- Temperature-Dependent Rotation of Protonated Methyl Groups in Otherwise Deuterated Proteins Modulates DEER Distance Distributions.Applied magnetic resonance · 2025Article
- Quantification of Rapid Cooling of Glycerol/Water Solutions Based on Photoluminescence from Thioflavin T.The journal of physical chemistry. B · 2024Article
- Optimization ofJournal of magnetic resonance (San Diego, Calif. : 1997) · 2024Article
- Deconvoluting Monomer- and Dimer-Specific Distance Distributions between Spin Labels in a Monomer/Dimer Mixture UsingJournal of the American Chemical Society · 2024Article
- Xplor-NIH: Better parameters and protocols for NMR protein structure determination.Protein science : a publication of the Protein Society · 2024Article
- Quantifying methyl tunneling induced (de)coherence of nitroxides in glassyPhysical chemistry chemical physics : PCCP · 2023Article
- Triggered Functional Dynamics of AsLOV2 by Time-Resolved Electron Paramagnetic Resonance at High Magnetic Fields.Angewandte Chemie (International ed. in English) · 2023Article
- Quantitative analysis of sterol-modulated monomer-dimer equilibrium of the βProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Binding and Functional Folding (BFF): A Physiological Framework for Studying Biomolecular Interactions and Allostery.Journal of molecular biology · 2022Review
- Combined Pulsed Electron Double Resonance EPR and Molecular Dynamics Investigations of Calmodulin Suggest Effects of Crowding Agents on Protein Structures.Biochemistry · 2022Article
- 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
- Time-resolved solid state NMR of biomolecular processes with millisecond time resolution.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2022Review
- 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
- Millisecond Time-Resolved Solid-State NMR Initiated by Rapid Inverse Temperature Jumps.Journal of the American Chemical Society · 2022Article
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6 authors at 1 institution in 1 country.
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Abstract
Recent advances in rapid mixing and freeze quenching have opened the path for time-resolved electron paramagnetic resonance (EPR)-based double electron-electron resonance (DEER) and solid-state NMR of protein-substrate interactions. DEER, in conjunction with phase memory time filtering to quantitatively extract species populations, permits monitoring time-dependent probability distance distributions between pairs of spin labels, while solid-state NMR provides quantitative residue-specific information on the appearance of structural order and the development of intermolecular contacts between substrate and protein. Here, we demonstrate the power of these combined approaches to unravel the kinetic and structural pathways in the binding of the intrinsically disordered peptide substrate (M13) derived from myosin light-chain kinase to the universal eukaryotic calcium regulator, calmodulin. Global kinetic analysis of the data reveals coupled folding and binding of the peptide associated with large spatial rearrangements of the two domains of calmodulin. The initial binding events involve a bifurcating pathway in which the M13 peptide associates via either its N- or C-terminal regions with the C- or N-terminal domains, respectively, of calmodulin/4Ca
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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.