Residue-Specific High-Resolution 17O Solid-State Nuclear Magnetic Resonance of Peptides: Multidimensional Indirect 1H Detection and Magic-Angle Spinning
Name
nihms-1868194.pdf
Description
Accepted version
Size
1.4 MB
Format
Adobe PDF
Checksum (MD5)
47d81ba2d0ec63ad3d94d3837d75ae1a
Author(s)
Hung, Ivan
Keeler, Eric G
Mao, Wenping
Gor’kov, Peter L
Griffin, Robert G
Gan, Zhehong
Date Issued
July 13, 2022
Journal
The Journal of Physical Chemistry Letters
Publisher
American Chemical Society
Citation
Residue-Specific High-Resolution 17O Solid-State Nuclear Magnetic Resonance of Peptides: Multidimensional Indirect 1H Detection and Magic-Angle Spinning. Ivan Hung, Eric G. Keeler, Wenping Mao, Peter L. Gor’kov, Robert G. Griffin, and Zhehong Gan. The Journal of Physical Chemistry Letters 2022 13 (28), 6549-6558.
Version
Author's final manuscript
Abstract
Oxygen is an integral component of proteins but remains sparsely studied because its only NMR active isotope, 17O, has low sensitivity, low resolution, and large quadrupolar couplings. These issues are addressed here with efficient isotopic labeling, high magnetic fields, fast sample spinning, and 1H detection in conjunction with multidimensional experiments to observe oxygen sites specific to each amino acid residue. Notably, cross-polarization at high sample spinning frequencies provides efficient 13C ↔ 17O polarization transfer. The use of 17O for initial polarization is found to provide better sensitivity per unit time compared to 1H. Sharp isotropic 17O peaks are obtained by using a low-power multiple-quantum sequence, which in turn allows extraction of quadrupolar parameters for each oxygen site. Finally, the potential to determine sequential assignments and long-range distance restraints is demonstrated by using 3D 1H/13C/17O experiments, suggesting that such methods can become an essential tool for biomolecular structure determination.
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DOI of Published Version
https://doi.org/10.1021/acs.jpclett.2c01777
