Journal
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
Volume 12, Issue 14, Pages 3679-3684Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpclett.1c00048
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Funding
- Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) under Germany's Excellence Strategy RESOLV [EXC 2033-390677874]
- European Research Council [669686]
- European Research Council (ERC) [669686] Funding Source: European Research Council (ERC)
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The study demonstrates the feasibility of using double electron-electron resonance (DEER) technique to measure distances between protein sites at very low protein concentrations, providing a new approach for studying conformational changes of biomolecules.
Electron paramagnetic resonance (EPR) spectroscopy is an established technique to site-specifically monitor conformational changes of spin-labeled biomolecules. Emerging in-cell EPR approaches aiming to address spin-labeled proteins in their native environment still struggle to reach a broad applicability and to target physiologically relevant protein concentrations. Here, we present a comparative in vitro and in-cell double electron-electron resonance (DEER) study demonstrating that nanomolar protein concentrations are at reach to measure distances up to 4.5 nm between protein sites carrying commercial gadolinium spin labels.
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