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Solid-state 17 O NMR of amino acids

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Solid-state 17 O NMR of amino acids. / Pike, K.J.; Lemaitre, V.; Kukol, A. et al.
In: Journal of Physical Chemistry B, Vol. 108, No. 26, 2004, p. 9256-9263.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

Harvard

Pike, KJ, Lemaitre, V, Kukol, A, Anupõld, T, Samoson, A, Howes, AP, Watts, A, Smith, ME & Dupree, R 2004, 'Solid-state 17 O NMR of amino acids', Journal of Physical Chemistry B, vol. 108, no. 26, pp. 9256-9263. https://doi.org/10.1021/jp049958x

APA

Pike, K. J., Lemaitre, V., Kukol, A., Anupõld, T., Samoson, A., Howes, A. P., Watts, A., Smith, M. E., & Dupree, R. (2004). Solid-state 17 O NMR of amino acids. Journal of Physical Chemistry B, 108(26), 9256-9263. https://doi.org/10.1021/jp049958x

Vancouver

Pike KJ, Lemaitre V, Kukol A, Anupõld T, Samoson A, Howes AP et al. Solid-state 17 O NMR of amino acids. Journal of Physical Chemistry B. 2004;108(26):9256-9263. doi: 10.1021/jp049958x

Author

Pike, K.J. ; Lemaitre, V. ; Kukol, A. et al. / Solid-state 17 O NMR of amino acids. In: Journal of Physical Chemistry B. 2004 ; Vol. 108, No. 26. pp. 9256-9263.

Bibtex

@article{253e693596b94b438ddd768e208051be,
title = "Solid-state 17 O NMR of amino acids",
abstract = "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/{\AA}) 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.",
keywords = "Carboxylic acids, Chemical bonds, Correlation methods, Hydrochloric acid, Nuclear magnetic resonance, Resonance, Solutions, Double-angle rotation (DOR), Dynamic angle spinning (DAS), Magic angle spinning (MAS), Amino acids",
author = "K.J. Pike and V. Lemaitre and A. Kukol and T. Anup{\~o}ld and A. Samoson and A.P. Howes and A. Watts and M.E. Smith and R. Dupree",
year = "2004",
doi = "10.1021/jp049958x",
language = "English",
volume = "108",
pages = "9256--9263",
journal = "Journal of Physical Chemistry B",
issn = "1520-6106",
publisher = "AMER CHEMICAL SOC",
number = "26",

}

RIS

TY - JOUR

T1 - Solid-state 17 O NMR of amino acids

AU - Pike, K.J.

AU - Lemaitre, V.

AU - Kukol, A.

AU - Anupõld, T.

AU - Samoson, A.

AU - Howes, A.P.

AU - Watts, A.

AU - Smith, M.E.

AU - Dupree, R.

PY - 2004

Y1 - 2004

N2 - 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.

AB - 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.

KW - Carboxylic acids

KW - Chemical bonds

KW - Correlation methods

KW - Hydrochloric acid

KW - Nuclear magnetic resonance

KW - Resonance

KW - Solutions

KW - Double-angle rotation (DOR)

KW - Dynamic angle spinning (DAS)

KW - Magic angle spinning (MAS)

KW - Amino acids

U2 - 10.1021/jp049958x

DO - 10.1021/jp049958x

M3 - Journal article

VL - 108

SP - 9256

EP - 9263

JO - Journal of Physical Chemistry B

JF - Journal of Physical Chemistry B

SN - 1520-6106

IS - 26

ER -