Distance Determination in Proteins inside Xenopus laevis Oocytes by Double Electron−Electron Resonance Experiments

DEER (double electron−electron resonance) enables the observation of long-range dipole interactions (1.5−8 nm) between electron spin centers and has become a unique method for structural analysis of site-directed spin-labeled (SDSL) proteins. The method was applied to proteins inside eukaryotic cell...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2010-06, Vol.132 (24), p.8228-8229
Main Authors: Igarashi, Ryuji, Sakai, Tomomi, Hara, Hideyuki, Tenno, Takeshi, Tanaka, Toshiaki, Tochio, Hidehito, Shirakawa, Masahiro
Format: Article
Language:English
Subjects:
Animals
Electron Spin Resonance Spectroscopy - methods
Feasibility Studies
Humans
Models, Molecular
Oocytes
Protein Conformation
Proteins - chemistry
Spin Labels
Ubiquitin - chemistry
Xenopus laevis
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Summary:DEER (double electron−electron resonance) enables the observation of long-range dipole interactions (1.5−8 nm) between electron spin centers and has become a unique method for structural analysis of site-directed spin-labeled (SDSL) proteins. The method was applied to proteins inside eukaryotic cells, Xenopus laevis oocytes. DEER measurements of the oocytes, into which SDSL-ubiquitin derivates were injected, gave rise to interpretable signals and allowed us to perform in situ analyses of the interspin distances of the proteins.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja906104e