Exploring Sulfur Sites in Proteins via Triple-Resonance 1H-Detected 77Se NMR

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Author(s)Koscielniak, Janusz
Author(s)Li, Jess
Author(s)Sail, Deepak
Author(s)Swenson, Rolf
Author(s)Anklin, Clemens
Author(s)Rozovsky, Sharon
Author(s)Byrd, R. Andrew
Date Accessioned2024-02-09T16:46:11Z
Date Available2024-02-09T16:46:11Z
Publication Date2023-11-15
DescriptionThis article was originally published in Journal of the American Chemical Society. The version of record is available at: https://doi.org/10.1021/jacs.3c07225. Copyright © 2023 The Authors. Published by American Chemical Society.
AbstractNMR spectroscopy has been applied to virtually all sites within proteins and biomolecules; however, the observation of sulfur sites remains very challenging. Recent studies have examined 77Se as a replacement for sulfur and applied 77Se NMR in both the solution and solid states. As a spin-1/2 nuclide, 77Se is attractive as a probe of sulfur sites, and it has a very large chemical shift range (due to a large chemical shift anisotropy), which makes it potentially very sensitive to structural and/or binding interactions as well as dynamics. Despite being a spin-1/2 nuclide, there have been rather limited studies of 77Se, and the ability to use 1H-indirect detection has been sparse. Some examples exist, but in the absence of a directly bonded, nonexchangeable 1H, these have been largely limited to smaller molecules. We develop and illustrate approaches using double-labeling of 13C and 77Se in proteins that enable more sensitive triple-resonance schemes via multistep coherence transfers and 1H-detection. These methods require specialized hardware and decoupling schemes, which we developed and will be discussed.
SponsorWe thank Wolfgang Bermel (Bruker BioSpin) for an initial loan of an NMR probe to test concepts and Ad Bax (NIDDK, NIH) for the donation of the Nalorac IDT3G600-5B probe used to construct the 1H/13C/77Se probe used in this work. We thank Dr. Toby Zens for discussions related to the probe reengineering. The authors acknowledge the use of the Biophysics Resource, Center for Structural Biology, NCI, and the assistance of Dr. Sergey Tarasov and Marzena Dyba. Funding: J.L. and R.A.B. are supported by the Intramural Research Program of the National Cancer Institute, Project ZIA BC 011132. J.K. is supported by Contract 75N91019D00024 to Leidos Biomedical Research, Inc. S.R. acknowledges support by the National Institutes of Health’s National Institute of General Medical Sciences under award GM121607, as well as the National Science Foundation under grant MCB-2150863. D.S. and R.S. are supported by the Intramural Research Program of the National Institutes of Health. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health, nor does mention of trade names, commercial products, or organizations imply endorsement by the U.S. Government.
CitationKoscielniak, Janusz, Jess Li, Deepak Sail, Rolf Swenson, Clemens Anklin, Sharon Rozovsky, and R. Andrew Byrd. “Exploring Sulfur Sites in Proteins via Triple-Resonance 1H-Detected 77Se NMR.” Journal of the American Chemical Society 145, no. 45 (November 15, 2023): 24648–56. https://doi.org/10.1021/jacs.3c07225.
ISSN1520-5126
URLhttps://udspace.udel.edu/handle/19716/33966
Languageen_US
PublisherJournal of the American Chemical Society
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
TitleExploring Sulfur Sites in Proteins via Triple-Resonance 1H-Detected 77Se NMR
TypeArticle
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