Studies of Proteins in Solution by Natural-Abundance Carbon-13 Nuclear Magnetic Resonance. Spectral Resolution and Relaxation Behavior at High Magnetic Field Strengths

Raymond S. Norton, Arthur O. Clouse, Robert Addleman, Adam Allerh

Research output: Contribution to journalArticleResearchpeer-review

77 Citations (Scopus)

Abstract

Natural-abundance 13C nuclear magnetic resonance spectra of hen egg-white lysozyme at 63.4 kG are compared with spectra at 14.2 kG. The increase in resolution when going from the low to the high field is much greater for aliphatic and methine aromatic carbon resonances than for carbonyl and nonprotonated aromatic carbon resonances. This result is consistent with experimental and calculated spin-lattice relaxation times, which demonstrate the dominance of chemical shift anisot-ropy as a relaxation mechanism for nonprotonated unsaturated carbons of a native protein at magnetic field strengths much above 40 kG. For the aliphatic and methine aromatic carbons, the 13C-1H dipolar relaxation mechanism should be dominant at all magnetic field strengths now available for NMR.

Original languageEnglish
Pages (from-to)79-83
Number of pages5
JournalJournal of the American Chemical Society
Volume99
Issue number1
DOIs
Publication statusPublished - 1977
Externally publishedYes

Cite this

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abstract = "Natural-abundance 13C nuclear magnetic resonance spectra of hen egg-white lysozyme at 63.4 kG are compared with spectra at 14.2 kG. The increase in resolution when going from the low to the high field is much greater for aliphatic and methine aromatic carbon resonances than for carbonyl and nonprotonated aromatic carbon resonances. This result is consistent with experimental and calculated spin-lattice relaxation times, which demonstrate the dominance of chemical shift anisot-ropy as a relaxation mechanism for nonprotonated unsaturated carbons of a native protein at magnetic field strengths much above 40 kG. For the aliphatic and methine aromatic carbons, the 13C-1H dipolar relaxation mechanism should be dominant at all magnetic field strengths now available for NMR.",
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Studies of Proteins in Solution by Natural-Abundance Carbon-13 Nuclear Magnetic Resonance. Spectral Resolution and Relaxation Behavior at High Magnetic Field Strengths. / Norton, Raymond S.; Clouse, Arthur O.; Addleman, Robert; Allerh, Adam.

In: Journal of the American Chemical Society, Vol. 99, No. 1, 1977, p. 79-83.

Research output: Contribution to journalArticleResearchpeer-review

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T1 - Studies of Proteins in Solution by Natural-Abundance Carbon-13 Nuclear Magnetic Resonance. Spectral Resolution and Relaxation Behavior at High Magnetic Field Strengths

AU - Norton, Raymond S.

AU - Clouse, Arthur O.

AU - Addleman, Robert

AU - Allerh, Adam

PY - 1977

Y1 - 1977

N2 - Natural-abundance 13C nuclear magnetic resonance spectra of hen egg-white lysozyme at 63.4 kG are compared with spectra at 14.2 kG. The increase in resolution when going from the low to the high field is much greater for aliphatic and methine aromatic carbon resonances than for carbonyl and nonprotonated aromatic carbon resonances. This result is consistent with experimental and calculated spin-lattice relaxation times, which demonstrate the dominance of chemical shift anisot-ropy as a relaxation mechanism for nonprotonated unsaturated carbons of a native protein at magnetic field strengths much above 40 kG. For the aliphatic and methine aromatic carbons, the 13C-1H dipolar relaxation mechanism should be dominant at all magnetic field strengths now available for NMR.

AB - Natural-abundance 13C nuclear magnetic resonance spectra of hen egg-white lysozyme at 63.4 kG are compared with spectra at 14.2 kG. The increase in resolution when going from the low to the high field is much greater for aliphatic and methine aromatic carbon resonances than for carbonyl and nonprotonated aromatic carbon resonances. This result is consistent with experimental and calculated spin-lattice relaxation times, which demonstrate the dominance of chemical shift anisot-ropy as a relaxation mechanism for nonprotonated unsaturated carbons of a native protein at magnetic field strengths much above 40 kG. For the aliphatic and methine aromatic carbons, the 13C-1H dipolar relaxation mechanism should be dominant at all magnetic field strengths now available for NMR.

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