ArticleChemistry (Weinheim an der Bergstrasse, Germany)2024
Endogenous Cu(II) Labeling for Distance Measurements on Proteins by EPR.
Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- EPR spectroscopy 80 years after its discovery.Science advances · 2026Review
- Binding Affinity Determines the Success of Endogenous CuThe journal of physical chemistry letters · 2026Article
- Electron Paramagnetic Resonance Spectroscopy Reveals Promoter Dependent Transcription Regulation by Copper Activated CueR in Pseudomonas aeruginosa.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Article
- Rational Design of a Cu(II) Spin Label Improves the Sensitivity of Distance Measurements.The journal of physical chemistry letters · 2025Article
- Recent advances in quantifying protein conformational ensembles with dipolar EPR spectroscopy.Current opinion in structural biology · 2025Review
- Q-Band Double Quantum Coherence ESR for Sensitive Nitroxide-Based Distance Measurements.The journal of physical chemistry. B · 2025Article
- Small Protein Domains as Potential Spin Labels for In Vitro, Cellular, and Light-Induced Dipolar EPR Spectroscopy.Journal of the American Chemical Society · 2025Article
- Exploring the Gating Mechanism of the Human Copper Transporter, hCtr1, Using EPR Spectroscopy.Biomolecules · 2025Article
- Endogenous Cu(II) Labeling for Distance Measurements on Proteins by EPR.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024Article
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Authors and funding
4 authors.
Funding
Abstract
In-cell measurements of the relationship between structure and dynamics to protein function is at the forefront of biophysics. Recently, developments in EPR methodology have demonstrated the sensitivity and power of this method to measure structural constraints in-cell. However, the need to spin label proteins ex-situ or use noncanonical amino acids to achieve endogenous labeling remains a bottleneck. In this work we expand the methodology to endogenously spin label proteins with Cu(II) spin labels and describe how to assess in-cell spin labeling. We quantify the amount of Cu(II)-NTA in cells, assess spin labeling, and account for orientational effects during distance measurements. We compare the efficacy of using heat-shock and hypotonic swelling to deliver spin label, showing that hypotonic swelling is a facile and reproducible method to efficiently deliver Cu(II)-NTA into E. coli. Notably, over six repeats we accomplish a bulk average of 57 μM spin labeled sites, surpassing existing endogenous labeling methods. The results of this work open the door for endogenous spin labeling that is easily accessible to the broader biophysical community.
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Registered trials
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.