Publikation: Combining site-directed spin labeling in vivo and in-cell EPR distance determination
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Physical Chemistry, Chemical Physics (PCCP). Royal Society of Chemistry (RSC). 2020, 22(9), pp. 4875-4879. ISSN 1463-9076. eISSN 1463-9084. Available under: doi: 10.1039/c9cp05584c
Zusammenfassung
Structural studies on proteins directly in their native environment are required for a comprehensive understanding of their function. Electron paramagnetic resonance (EPR) spectroscopy and in particular double electron-electron resonance (DEER) distance determination are suited to investigate spin-labeled proteins directly in the cell. The combination of intracellular bioorthogonal labeling with in-cell DEER measurements does not require additional purification or delivery steps of spin-labeled protein to the cells. In this study, we express eGFP in E. coli and use copper-catalyzed azide-alkyne cycloaddition (CuAAC) for the site-directed spin labeling of the protein in vivo, followed by in-cell EPR distance determination. Inter-spin distance measurements of spin-labeled eGFP agree with in vitro measurements and calculations based on the rotamer library of the spin label.
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WIDDER, Pia, Julian SCHUCK, Daniel SUMMERER, Malte DRESCHER, 2020. Combining site-directed spin labeling in vivo and in-cell EPR distance determination. In: Physical Chemistry, Chemical Physics (PCCP). Royal Society of Chemistry (RSC). 2020, 22(9), pp. 4875-4879. ISSN 1463-9076. eISSN 1463-9084. Available under: doi: 10.1039/c9cp05584cBibTex
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year={2020},
doi={10.1039/c9cp05584c},
title={Combining site-directed spin labeling in vivo and in-cell EPR distance determination},
number={9},
volume={22},
issn={1463-9076},
journal={Physical Chemistry, Chemical Physics (PCCP)},
pages={4875--4879},
author={Widder, Pia and Schuck, Julian and Summerer, Daniel and Drescher, Malte}
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<dcterms:abstract xml:lang="eng">Structural studies on proteins directly in their native environment are required for a comprehensive understanding of their function. Electron paramagnetic resonance (EPR) spectroscopy and in particular double electron-electron resonance (DEER) distance determination are suited to investigate spin-labeled proteins directly in the cell. The combination of intracellular bioorthogonal labeling with in-cell DEER measurements does not require additional purification or delivery steps of spin-labeled protein to the cells. In this study, we express eGFP in E. coli and use copper-catalyzed azide-alkyne cycloaddition (CuAAC) for the site-directed spin labeling of the protein in vivo, followed by in-cell EPR distance determination. Inter-spin distance measurements of spin-labeled eGFP agree with in vitro measurements and calculations based on the rotamer library of the spin label.</dcterms:abstract>
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