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  Spatiotemporal resolution of conformational changes in biomolecules by combining pulsed electron–electron double resonance spectroscopy with microsecond freeze-hyperquenching

Hett, T., Zbik, T., Mukherjee, S., Matsuoka, H., Bönigk, W., Klose, D., et al. (2021). Spatiotemporal resolution of conformational changes in biomolecules by combining pulsed electron–electron double resonance spectroscopy with microsecond freeze-hyperquenching. Journal of the American Chemical Society, 143(18), 6981-6989. doi:10.1021/jacs.1c01081.

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Hett, T., Author
Zbik, T., Author
Mukherjee, S., Author
Matsuoka, H., Author
Bönigk, W., Author
Klose, D., Author
Rouillon, C., Author
Brenner, N., Author
Peuker, S., Author
Klement, R.1, Author              
Steinhoff, H.-J., Author
Grubmüller, H.2, Author              
Seifert, R., Author
Schiemann, O., Author
Kaupp, U. B., Author
Affiliations:
1Department of Theoretical and Computational Biophysics, MPI for Biophysical Chemistry, Max Planck Society, ou_578631              
2Department of Theoretical and Computational Biophysics, MPI for biophysical chemistry, Max Planck Society, ou_578631              

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 Abstract: The function of proteins is linked to their conformations that can be resolved with several high-resolution methods. However, only a few methods can provide the temporal order of intermediates and conformational changes, with each having its limitations. Here, we combine pulsed electron–electron double resonance spectroscopy with a microsecond freeze-hyperquenching setup to achieve spatiotemporal resolution in the angstrom range and lower microsecond time scale. We show that the conformational change of the Cα-helix in the cyclic nucleotide-binding domain of the Mesorhizobium loti potassium channel occurs within about 150 μs and can be resolved with angstrom precision. Thus, this approach holds great promise for obtaining 4D landscapes of conformational changes in biomolecules.

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Language(s): eng - English
 Dates: 2021-04-272021-05-12
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: DOI: 10.1021/jacs.1c01081
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Title: Journal of the American Chemical Society
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Source Genre: Journal
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Pages: - Volume / Issue: 143 (18) Sequence Number: - Start / End Page: 6981 - 6989 Identifier: -