ArticleBiochemical and biophysical research communications2014
Continuous wave W- and D-band EPR spectroscopy offer "sweet-spots" for characterizing conformational changes and dynamics in intrinsically disordered proteins.
Article in Biochemical and biophysical research communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 23 citations in OpenAlex.
- CW ESR spectroscopy and protein spin labeling in membrane biology.Physical biology · 2025Review
- Core-shell model of the clusters of CPEB4 isoforms preceding liquid-liquid phase separation.Biophysical journal · 2024Article
- Spin-labeling Insights into How Chemical Fixation Impacts Glycan Organization on Cells.Applied magnetic resonance · 2024Article
- Evolution of CPEB4 Dynamics Across its Liquid-Liquid Phase Separation Transition.The journal of physical chemistry. B · 2021Article
- A metabolically engineered spin-labeling approach for studying glycans on cells.Chemical science · 2020Article
- Exploring intrinsically disordered proteins using site-directed spin labeling electron paramagnetic resonance spectroscopy.Frontiers in molecular biosciences · 2015Review
- Determining the Secondary Structure of Membrane Proteins and Peptides Via Electron Spin Echo Envelope Modulation (ESEEM) Spectroscopy.Methods in enzymology · 2015Article
- Spin labeling and Double Electron-Electron Resonance (DEER) to Deconstruct Conformational Ensembles of HIV Protease.Methods in enzymology · 2015Article
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6 authors at 1 institution in 1 country.
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Abstract
Site-directed spin labeling (SDSL) electron paramagnetic resonance (EPR) spectroscopy is a powerful tool for characterizing conformational sampling and dynamics in biological macromolecules. Here we demonstrate that nitroxide spectra collected at frequencies higher than X-band (∼9.5 GHz) have sensitivity to the timescale of motion sampled by highly dynamic intrinsically disordered proteins (IDPs). The 68 amino acid protein IA3, was spin-labeled at two distinct sites and a comparison of X-band, Q-band (35 GHz) and W-band (95 GHz) spectra are shown for this protein as it undergoes the helical transition chemically induced by tri-fluoroethanol. Experimental spectra at W-band showed pronounced line shape dispersion corresponding to a change in correlation time from ∼0.3 ns (unstructured) to ∼0.6 ns (α-helical) as indicated by comparison with simulations. Experimental and simulated spectra at X- and Q-bands showed minimal dispersion over this range, illustrating the utility of SDSL EPR at higher frequencies for characterizing structural transitions and dynamics in IDPs.
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