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dc.contributor.authorKeeler, Eric George
dc.contributor.authorMichaelis, Vladimir K.
dc.contributor.authorColvin, Michael Thomas
dc.contributor.authorHung, Ivan
dc.contributor.authorGor’kov, Peter L.
dc.contributor.authorCross, Timothy A.
dc.contributor.authorGan, Zhehong
dc.contributor.authorGriffin, Robert Guy
dc.date.accessioned2020-02-28T19:29:03Z
dc.date.available2020-02-28T19:29:03Z
dc.date.issued2017-11
dc.date.submitted2017-08
dc.identifier.issn0002-7863
dc.identifier.issn1520-5126
dc.identifier.urihttps://hdl.handle.net/1721.1/123892
dc.description.abstractThe 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.en_US
dc.description.sponsorshipNational Institutes of Health (U.S.) (Grant EB-001960)en_US
dc.description.sponsorshipNational Institutes of Health (U.S.) (Grant EB-002804)en_US
dc.description.sponsorshipNational Institutes of Health (U.S.) (Grant EB-002026)en_US
dc.language.isoen_US
dc.publisherAmerican Chemical Society (ACS)en_US
dc.relation.isversionofhttp://dx.doi.org/10.1021/jacs.7b08989en_US
dc.rightsArticle 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.en_US
dc.sourceProf. Griffin via Erja Kajosaloen_US
dc.title¹⁷O MAS NMR Correlation Spectroscopy at High Magnetic Fieldsen_US
dc.typeArticleen_US
dc.identifier.citationKeeler, 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 Societyen_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Chemistryen_US
dc.contributor.approverGriffin, Robert Guyen_US
dc.relation.journalJournal of the American Chemical Societyen_US
dc.eprint.versionAuthor's final manuscripten_US
dc.type.urihttp://purl.org/eprint/type/JournalArticleen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dspace.orderedauthorsKeeler, Eric G.; Michaelis, Vladimir K.; Colvin, Michael T.; Hung, Ivan; Gor’kov, Peter L.; Cross, Timothy A.; Gan, Zhehong; Griffin, Robert G.en_US
dspace.embargo.termsNen_US
dspace.date.submission2019-04-04T13:20:46Z
mit.journal.volume139en_US
mit.journal.issue49en_US
mit.licensePUBLISHER_POLICYen_US


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