¹⁷O MAS NMR Correlation Spectroscopy at High Magnetic Fields
Author(s)
Keeler, Eric George
Michaelis, Vladimir K.
Colvin, Michael Thomas
Hung, Ivan
Gor’kov, Peter L.
Cross, Timothy A.
Gan, Zhehong
Griffin, Robert Guy
Date Issued
November 2017
Journal
Journal of the American Chemical Society
Publisher
American Chemical Society (ACS)
Citation
Keeler, Eric G. et al. “¹⁷O MAS NMR Correlation Spectroscopy at High Magnetic Fields.” Journal of the American Chemical Society 139, 49 (November 2017): 17953–17963 © 2017 American Chemical Society
Version
Author's final manuscript
Abstract
The structure of two protected amino acids, FMOC-l-leucine and FMOC-l-valine, and a dipeptide, N-acetyl-l-valyl-l-leucine (N-Ac-VL), were studied via one- and two-dimensional solid-state nuclear magnetic resonance (NMR) spectroscopy. Utilizing ¹⁷O magic-angle spinning (MAS) NMR at multiple magnetic fields (17.6–35.2 T/750–1500 MHz for 1H) the ¹⁷O quadrupolar and chemical shift parameters were determined for the two oxygen sites of each FMOC-protected amino acids and the three distinct oxygen environments of the dipeptide. The one- and two-dimensional, ¹⁷O, ¹⁵N–¹⁷O, ¹³C–¹⁷O, and 1H–¹⁷O double-resonance correlation experiments performed on the uniformly ¹³C,¹⁵N and 70% ¹⁷O-labeled dipeptide prove the attainability of ¹⁷O as a probe for structure studies of biological systems. ¹⁵N–¹⁷O and ¹³C–¹⁷O distances were measured via one-dimensional REAPDOR and ZF-TEDOR experimental buildup curves and determined to be within 15% of previously reported distances, thus demonstrating the use of ¹⁷O NMR to quantitate interatomic distances in a fully labeled dipeptide. Through-space hydrogen bonding of N-Ac-VL was investigated by a two-dimensional ¹H-detected ¹⁷O R³-R-INEPT experiment, furthering the importance of ¹⁷O for studies of structure in biomolecular solids.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
Terms of Use
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Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1021/jacs.7b08989
