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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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Item Permalink: https://hdl.handle.net/21.11116/0000-0008-7179-1 Version Permalink: https://hdl.handle.net/21.11116/0000-000D-5412-0
Genre: Journal Article

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https://pubs.acs.org/doi/10.1021/jacs.1c01081 (Publisher version)
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 Creators:
Hett, Tobias1, Author
Zbik, Tobias2, Author
Mukherjee, Shatanik2, Author           
Matsuoka, Hideto1, Author
Bönigk, Wolfgang2, Author           
Klose, Daniel1, Author
Rouillon, Christophe2, Author           
Brenner, Norbert2, Author
Peuker, Sebastian2, Author           
Klement, Reinhard1, Author
Steinhoff, Heinz-Jürgen1, Author
Grubmüller, Helmut1, Author
Seifert, Reinhard2, Author           
Schiemann, Olav1, Author
Kaupp, Ulrich Benjamin2, Author           
Affiliations:
1External Organizations, ou_persistent22              
2Department of Molecular Sensory Systems, Center of Advanced European Studies and Research (caesar), Max Planck Society, ou_2173679              

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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
 Publication Status: Issued
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 Rev. Type: Peer
 Identifiers: DOI: 10.1021/jacs.1c01081
PMID: 33905249
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Title: Journal of the American Chemical Society
  Abbreviation : J Am Chem Soc
Source Genre: Journal
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Publ. Info: Washington, DC : American Chemical Society
Pages: - Volume / Issue: 143 (18) Sequence Number: - Start / End Page: 6981 - 6989 Identifier: ISSN: 0002-7863
CoNE: https://pure.mpg.de/cone/journals/resource/954925376870