¹⁷O MAS NMR Correlation Spectroscopy at High Magnetic Fields
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...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | en_US |
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American Chemical Society (ACS)
2020
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| Online Access: | https://hdl.handle.net/1721.1/123892 |
| _version_ | 1811080945174839296 |
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| author | Keeler, Eric George Michaelis, Vladimir K. Colvin, Michael Thomas Hung, Ivan Gor’kov, Peter L. Cross, Timothy A. Gan, Zhehong Griffin, Robert Guy |
| author2 | Massachusetts Institute of Technology. Department of Chemistry |
| author_facet | Massachusetts Institute of Technology. Department of Chemistry Keeler, Eric George Michaelis, Vladimir K. Colvin, Michael Thomas Hung, Ivan Gor’kov, Peter L. Cross, Timothy A. Gan, Zhehong Griffin, Robert Guy |
| author_sort | Keeler, Eric George |
| collection | MIT |
| description | 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. |
| first_indexed | 2024-09-23T11:39:20Z |
| format | Article |
| id | mit-1721.1/123892 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T11:39:20Z |
| publishDate | 2020 |
| publisher | American Chemical Society (ACS) |
| record_format | dspace |
| spelling | mit-1721.1/1238922022-10-01T05:04:32Z ¹⁷O MAS NMR Correlation Spectroscopy at High Magnetic Fields Keeler, Eric George Michaelis, Vladimir K. Colvin, Michael Thomas Hung, Ivan Gor’kov, Peter L. Cross, Timothy A. Gan, Zhehong Griffin, Robert Guy Massachusetts Institute of Technology. Department of Chemistry Griffin, Robert Guy 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. National Institutes of Health (U.S.) (Grant EB-001960) National Institutes of Health (U.S.) (Grant EB-002804) National Institutes of Health (U.S.) (Grant EB-002026) 2020-02-28T19:29:03Z 2020-02-28T19:29:03Z 2017-11 2017-08 Article http://purl.org/eprint/type/JournalArticle 0002-7863 1520-5126 https://hdl.handle.net/1721.1/123892 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 en_US http://dx.doi.org/10.1021/jacs.7b08989 Journal of the American Chemical Society Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. application/octet-stream application/pdf American Chemical Society (ACS) Prof. Griffin via Erja Kajosalo |
| spellingShingle | Keeler, Eric George Michaelis, Vladimir K. Colvin, Michael Thomas Hung, Ivan Gor’kov, Peter L. Cross, Timothy A. Gan, Zhehong Griffin, Robert Guy ¹⁷O MAS NMR Correlation Spectroscopy at High Magnetic Fields |
| title | ¹⁷O MAS NMR Correlation Spectroscopy at High Magnetic Fields |
| title_full | ¹⁷O MAS NMR Correlation Spectroscopy at High Magnetic Fields |
| title_fullStr | ¹⁷O MAS NMR Correlation Spectroscopy at High Magnetic Fields |
| title_full_unstemmed | ¹⁷O MAS NMR Correlation Spectroscopy at High Magnetic Fields |
| title_short | ¹⁷O MAS NMR Correlation Spectroscopy at High Magnetic Fields |
| title_sort | ¹⁷o mas nmr correlation spectroscopy at high magnetic fields |
| url | https://hdl.handle.net/1721.1/123892 |
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