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, A. O.; Addleman, Robert; Allerhand, Adam

doi:10.1021/ja00443a016

Cited by 87 publications

(59 citation statements)

References 8 publications

(10 reference statements)

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“…The results for these two different proton chemical shifts were the same within the experimental error, with Tl = 0.24+0.04 s and T 2 = 0.16+0.03 s. These values yield an estimate for the correlation time ~o equal to 1.1 +0.5 ns, based on a pure dipoledipole relaxation mechanism dominated by the directly attached proton. As demonstrated for other proteins [32], the chemical shift anisotropy relaxation mechanism for the s-carbons of proteins contributes an insignificant amount to the 13C relaxation times T~ and T2 in this range of correlation times.…”

Section: Calculation Of R~mentioning

confidence: 51%

Solution structure of ω‐conotoxin MVIIA using 2D NMR spectroscopy

Basus¹,

Nádasdi²,

Ramachandran³

et al. 1995

FEBS Letters

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The solution structure of ~-conotoxin MVIIA (SNX-111), a peptide toxin from the fish hunting cone snail Conus magus and a high-affinity blocker of N-type calcium channels, was determined by 2D NMR spectroscopy. The backbones of the best 44 structures match with an average pairwise RMSD of 0.59 angstroms. The structures contain a short segment of triplestranded t-sheet involving residues 6-8, 20-21, and 24-25. The structure of this toxin is very similar to that of ¢o-conotoxin GVIA with which is has only 40% sequence homology, but very similar calcium channel binding affinity and selectivity.

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Section: Calculation Of R~mentioning

confidence: 51%

Solution structure of ω‐conotoxin MVIIA using 2D NMR spectroscopy

Basus¹,

Nádasdi²,

Ramachandran³

et al. 1995

FEBS Letters

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“…At present it is not possible to assess the molecular motions from relaxation measurements of carboxyl resonances because the 13C relaxation mechanism of the carboxyl carbon is not known (4). However, '3C relaxation of protonated carbons occurs via 13C-1H dipolar interactions at magnetic fields comparable with that used in this study (19).…”

Section: Aqueousmentioning

confidence: 69%

Interactions of myristic acid with bovine serum albumin: a 13C NMR study.

Hamilton¹,

Cistola²,

Morrisett³

et al. 1984

Proc. Natl. Acad. Sci. U.S.A.

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Interactions of myristic acid with bovine serum albumin were studied by 13C NMR spectroscoy at 50.3 MHz using 90% isotopically substituted [1-'3C1-, [3-C] 13C]myristic acid to bovine serum albumin (from 0.7 to 5.6) revealed at least two narrow resonances for each carbon at all molar ratios. Thus, bovine serum albumin binding sites for myristic acid are heterogeneous with respect to titration behavior and with respect to the local magnetic environment at both the polar and the nonpolar ends of the fatty acid. The narrow resonances observed for the methylene and methyl carbons are inconsistent with complete immobilization of the protein-bound acid molecules. Together with spin-lattice relaxation times and nuclear Overhauser enhancements, the linewidth results indicate that bound myristic acid has internal motions that are rapid compared with overall protein tumbling and that the C-3 methylene carbon is more restricted than the terminal methyl carbon.

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“…In contrast, few, if any, of the aliphatic carbons yield resolved individual-carbon resonances, even at a magnetic field strength as high as 63.4 kg [4]. We show in this report that the trimethylammonium group of the single e-N-trimethyllysine residue of Candida krusei cytochrome c [5,6] yields an identifiable narrow individual-carbon resonance in the region of the relatively broad u-carbon resonances.…”

Section: Introductionmentioning

confidence: 58%