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  High-field dipolar electron paramagnetic resonance (EPR) spectroscopy of nitroxide biradicals for determining three-dimensional structures of biomacromolecules in disordered solids

Savitsky, A., Dubinskii, A. A. A., Zimmermann, H., Lubitz, W., & Möbius, K. (2011). High-field dipolar electron paramagnetic resonance (EPR) spectroscopy of nitroxide biradicals for determining three-dimensional structures of biomacromolecules in disordered solids. The Journal of Physical Chemistry B, 115(41), 11950-11963. doi:10.1021/jp206841v.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-1EEE-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-1EEF-8
Genre: Journal Article
Alternative Title : High-field dipolar electron paramagnetic resonance (EPR) spectroscopy of nitroxide biradicals for determining three-dimensional structures of biomacromolecules in disordered solids

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Savitsky, Anton, Author
Dubinskii, Alexander A. A., Author
Zimmermann, Herbert1, 2, Author              
Lubitz, Wolfgang, Author
Möbius, Klaus, Author
Affiliations:
1Department of Molecular Physics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497705              
2Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 Abstract: We consider the state−of−the−art capabilities and future perspectives of electron−spin triangulation by high−field/high−frequency dipolar electron paramagnetic resonance (EPR) techniques designed for determining the three−dimensional structure of large supra−molecular complexes dissolved in disordered solids. These techniques combine double site−directed spin labeling (SDSL) with orientation−resolving pulsed electron−electron double resonance (PELDOR) spectroscopy. In particular, we appraise the prospects of angular triangulation, which extends the more familiar distance triangulation. As a model case for spin−labeled proteins, the three−dimensional structures of two nitroxide biradicals with rather stiff bridging blocks and deuterated nitroxide headgroups have been derived. To this end we applied 95 GHz high−field electron dipolar EPR spectroscopy with the microwave pulse−sequence configurations for PELDOR and relaxation−induced dipolar modulation enhancement (RIDME). Various specific spectroscopic strategies are discussed to overcome the problems of overlapping spectra of the chemically identical nitroxide labels when attached to macromolecular systems. We conclude that due to the high detection sensitivity and spectral resolution the combination of SDSL with high−field RIDME/PELDOR stands out as an extremely powerful tool for 3D structure determination of large disordered systems. The approach compares favorably with other structure−determining magnetic−resonance methods. This holds true both for stable and transient radical−pair states. Angular constraints are provided in addition to distance constraints obtained for the same sample. Thereby, the number of necessary distance constraints is strongly reduced. Since each measurement of a distance constraint requires an additional doubly spin−labeled sample, the reduction of necessary distance constraints is another appealing aspect of orientation−resolving EPR spin triangulation for protein structure determination

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Language(s): eng - English
 Dates: 2011-08-312011-07-182011-08-312011-09-272011-10-20
 Publication Status: Published in print
 Pages: 14
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 Rev. Method: Peer
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Title: The Journal of Physical Chemistry B
  Other : J. Phys. Chem. B
Source Genre: Journal
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Publ. Info: Washington, D.C. : American Chemical Society
Pages: - Volume / Issue: 115 (41) Sequence Number: - Start / End Page: 11950 - 11963 Identifier: ISSN: 1520-6106
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000293370_1