ArticleProceedings of the National Academy of Sciences of the United States of America2020
Spin-labeled nanobodies as protein conformational reporters for electron paramagnetic resonance in cellular membranes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 53 citations in OpenAlex.
- Capturing transient states of heterodimeric ABC transporter TM287/288 by time-resolved small-angle X-ray scattering.Biophysical journal · 2026Article
- Protocol for preparing and characterizing samples for combined microsecond freeze-hyperquenching and electron paramagnetic resonance spectroscopy.STAR protocols · 2026Article
- Modeling protein conformational ensembles by guiding AlphaFold2 with Double Electron Electron Resonance (DEER) distance distributions.Nature communications · 2025Article
- Q-Band Double Quantum Coherence ESR for Sensitive Nitroxide-Based Distance Measurements.The journal of physical chemistry. B · 2025Article
- Pulse Dipolar Electron Paramagnetic Resonance Spectroscopy Distance Measurements at Low Nanomolar Concentrations: The CuThe journal of physical chemistry letters · 2024Article
- Spectroscopically Orthogonal Labelling to Disentangle Site-Specific Nitroxide Label Distributions.Applied magnetic resonance · 2024Article
- Conformational Heterogeneity of β-Barrel Membrane Proteins Observed In Situ Using Orthogonal Spin Labels and Pulsed ESR Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Double Quantum Coherence ESR at Q-Band Enhances the Sensitivity of Distance Measurements at Submicromolar Concentrations.The journal of physical chemistry letters · 2023Article
- Profound Changes in Functional Structure and Dynamics of Serum Albumin in Children with Nephrotic Syndrome: An Exploratory Research Study.Journal of medicinal chemistry · 2023Article
- Ultrafast Bioorthogonal Spin-Labeling and Distance Measurements in Mammalian Cells Using Small, Genetically Encoded Tetrazine Amino Acids.Journal of the American Chemical Society · 2023Article
- Perspective on the Effect of Membrane Mimetics on Dynamic Properties of Integral Membrane Proteins.The journal of physical chemistry. B · 2023Review
- Dance with spins: site-directed spin labeling coupled to electron paramagnetic resonance spectroscopy directly inside cells.Chemical communications (Cambridge, England) · 2023Review
- Ultra-Fast Bioorthogonal Spin-Labeling and Distance Measurements in Mammalian Cells Using Small, Genetically Encoded Tetrazine Amino Acids.bioRxiv : the preprint server for biology · 2023Article
- The ABC transporter MsbA adopts the wide inward-open conformation inScience advances · 2022Article
- Cross-validation of distance measurements in proteins by PELDOR/DEER and single-molecule FRET.Nature communications · 2022Article
- Conformational Flexibility of the Protein Insertase BamA in the Native Asymmetric Bilayer Elucidated by ESR Spectroscopy.Angewandte Chemie (International ed. in English) · 2022Article
- Uptake of Cell-Penetrating Peptide RL2 by Human Lung Cancer Cells: Monitoring by Electron Paramagnetic Resonance and Confocal Laser Scanning Microscopy.Molecules (Basel, Switzerland) · 2021Article
- Substrate binding in the multidrug transporter MdfA in detergent solution and in lipid nanodiscs.Biophysical journal · 2021Article
- Review
- Protein Conformational Dynamics upon Association with the Surfaces of Lipid Membranes and Engineered Nanoparticles: Insights from Electron Paramagnetic Resonance Spectroscopy.Molecules (Basel, Switzerland) · 2020Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nanobodies are emerging tools in a variety of fields such as structural biology, cell imaging, and drug discovery. Here we pioneer the use of their spin-labeled variants as reporters of conformational dynamics of membrane proteins using DEER spectroscopy. At the example of the bacterial ABC transporter TM287/288, we show that two gadolinium-labeled nanobodies allow us to quantify, via analysis of the modulation depth of DEER traces, the fraction of transporters adopting the outward-facing state under different experimental conditions. Additionally, we quantitatively follow the interconversion from the outward- to the inward-facing state in the conformational ensemble under ATP turnover conditions. We finally show that the specificity of the nanobodies for the target protein allows the direct attainment of structural information on the wild-type TM287/288 expressed in cellular membranes without the need to purify or label the investigated membrane protein.
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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.