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Tracking protein domain movements by EPR distance determination and multilateration

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2022

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Methods in enzymology. Elsevier. 2022, 666, pp. 121-144. ISSN 0076-6879. eISSN 1557-7988. Available under: doi: 10.1016/bs.mie.2022.02.016

Zusammenfassung

Electron paramagnetic resonance (EPR) spectroscopy in combination with site-directed spin labeling (SDSL) is a powerful approach to supplement the large toolbox of methods for protein structure determination. The strength of EPR spectroscopy is the ability to map flexibility of protein domains and conformational ensembles. EPR distance determination in the nanometer range and subsequent multilateration enables the three-dimensional visualization of the localization of a spin label in a protein domain. Therefore, multilateration can not only be used to represent the degree of flexibility of protein structural elements, but also track movements of whole domains. We report a detailed protocol for all needed steps, beginning with the choice of the labeling sites, the spin labeling reaction, the EPR distance measurement by double electron-electron resonance (DEER) and finally the multilateration exploiting the EPR distance restraints.

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540 Chemie

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EPR spectroscopy, DEER Multilateration, Trilateration Kinase, Conformational change

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ISO 690STEHLE, Juliane, Malte DRESCHER, 2022. Tracking protein domain movements by EPR distance determination and multilateration. In: Methods in enzymology. Elsevier. 2022, 666, pp. 121-144. ISSN 0076-6879. eISSN 1557-7988. Available under: doi: 10.1016/bs.mie.2022.02.016
BibTex
@article{Stehle2022Track-59585,
  year={2022},
  doi={10.1016/bs.mie.2022.02.016},
  title={Tracking protein domain movements by EPR distance determination and multilateration},
  volume={666},
  issn={0076-6879},
  journal={Methods in enzymology},
  pages={121--144},
  author={Stehle, Juliane and Drescher, Malte}
}
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