Solid-state O-17 NMR of amino acids
17 O solid-state NMR from 14 amino acids is reported here, greatly increasing the number investigated. In most cases well-separated resonances from carbonyl and hydroxyl oxygens with distinct second-order quadrupolar line shapes are observed using a 600 MHz spectrometer with fast magic angle spinnin...
| Main Authors: | , , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2004
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| _version_ | 1797078077038133248 |
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| author | Pike, K Lemaitre, V Kukol, A Anupold, T Samoson, A Howes, A Watts, A Smith, M Dupree, R |
| author_facet | Pike, K Lemaitre, V Kukol, A Anupold, T Samoson, A Howes, A Watts, A Smith, M Dupree, R |
| author_sort | Pike, K |
| collection | OXFORD |
| description | 17 O solid-state NMR from 14 amino acids is reported here, greatly increasing the number investigated. In most cases well-separated resonances from carbonyl and hydroxyl oxygens with distinct second-order quadrupolar line shapes are observed using a 600 MHz spectrometer with fast magic angle spinning (MAS). This is in contrast to the motionally averaged resonances usually seen from amino acids in solution. For amino acids double-angle rotation (DOR) produces a decrease in the line width by more than a factor of 40, providing very high resolution, ∼ 1 ppm, spectra. The oxygen lines in alanine and the carbonyl oxygens in L-glutamic acid hydrochloride are assigned using 1H-decoupled DOR. The NMR interaction parameters for amino acids show a wide variation of XQ, from 6.4 to 8.6 MHz, η from 0.0 to 0.9, and δiso from 83 to 353 ppm. The high quality of the MAS NMR line shapes obtained at 14.1 T means that even small changes in parameters can be very accurately deduced, offering the possibility of 17O NMR as a sensitive probe of structural changes in these and related compounds. The D- and L-forms of glutamic acid hydrochloride are shown to have the same NMR parameters to within error, which are very different from those reported in the literature for the D,L-form. A strong correlation (∼-1200 ppm/Å) is found between δiso and the C-O bond length of the carbonyl oxygens. On the basis of these data, enriching specific amino acids in more complex polypeptides and proteins could provide site-selective information about the bonding and functionality of different sites in biomolecules. An estimate is made of the possible detection limit for such species. |
| first_indexed | 2024-03-07T00:27:18Z |
| format | Journal article |
| id | oxford-uuid:7e931df8-4791-4929-b4f9-9c000ddc18bf |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T00:27:18Z |
| publishDate | 2004 |
| record_format | dspace |
| spelling | oxford-uuid:7e931df8-4791-4929-b4f9-9c000ddc18bf2022-03-26T21:10:57ZSolid-state O-17 NMR of amino acidsJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:7e931df8-4791-4929-b4f9-9c000ddc18bfEnglishSymplectic Elements at Oxford2004Pike, KLemaitre, VKukol, AAnupold, TSamoson, AHowes, AWatts, ASmith, MDupree, R17 O solid-state NMR from 14 amino acids is reported here, greatly increasing the number investigated. In most cases well-separated resonances from carbonyl and hydroxyl oxygens with distinct second-order quadrupolar line shapes are observed using a 600 MHz spectrometer with fast magic angle spinning (MAS). This is in contrast to the motionally averaged resonances usually seen from amino acids in solution. For amino acids double-angle rotation (DOR) produces a decrease in the line width by more than a factor of 40, providing very high resolution, ∼ 1 ppm, spectra. The oxygen lines in alanine and the carbonyl oxygens in L-glutamic acid hydrochloride are assigned using 1H-decoupled DOR. The NMR interaction parameters for amino acids show a wide variation of XQ, from 6.4 to 8.6 MHz, η from 0.0 to 0.9, and δiso from 83 to 353 ppm. The high quality of the MAS NMR line shapes obtained at 14.1 T means that even small changes in parameters can be very accurately deduced, offering the possibility of 17O NMR as a sensitive probe of structural changes in these and related compounds. The D- and L-forms of glutamic acid hydrochloride are shown to have the same NMR parameters to within error, which are very different from those reported in the literature for the D,L-form. A strong correlation (∼-1200 ppm/Å) is found between δiso and the C-O bond length of the carbonyl oxygens. On the basis of these data, enriching specific amino acids in more complex polypeptides and proteins could provide site-selective information about the bonding and functionality of different sites in biomolecules. An estimate is made of the possible detection limit for such species. |
| spellingShingle | Pike, K Lemaitre, V Kukol, A Anupold, T Samoson, A Howes, A Watts, A Smith, M Dupree, R Solid-state O-17 NMR of amino acids |
| title | Solid-state O-17 NMR of amino acids |
| title_full | Solid-state O-17 NMR of amino acids |
| title_fullStr | Solid-state O-17 NMR of amino acids |
| title_full_unstemmed | Solid-state O-17 NMR of amino acids |
| title_short | Solid-state O-17 NMR of amino acids |
| title_sort | solid state o 17 nmr of amino acids |
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