Natural abundance nitrogen-15 nuclear magnetic resonance spectroscopy—amino-acid derivatives

Pregosin, Paul S.; Randall, E. W.; White, A. I.

doi:10.1039/c29710001602

Cited by 26 publications

(5 citation statements)

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“…On the other hand, the 51 residues N-terminal part of the ~rotein shows narrow 1~ resonance lines ( Figure 1) and is quite suitable for conducting ~ NMR studies of specific interaction of the lac repressor with its operator . On the basis of their chemical shift, they were tentatively assigned to 1~ of arginine residues (45)(46)(47)(48). The glutamine and asparagine side-chain 1~2 groups appear as two peaks at a common 15 N chemical shift as indicated by the horizontal lines.…”

mentioning

confidence: 99%

Two-Dimensional¹H,¹⁵N NMR investigation of uniformly¹⁵N-labeledLacRepressor Headpiece

Lancelot

Gervais

Maurizot

1992

Journal of Biomolecular Structure and Dynamics

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15N uniformly labeled lac repressor and lac repressor headpiece were prepared. 15N NMR spectra of lac repressor were shown resolution inadequate for detailed study while the data showed that the 15N labeled N-terminal part of the protein is quite suitable for this type of study allowing future investigation of the specific interaction of the lac repressor headpiece with the lac operator. We report here the total assignment of proton 1H and nitrogen 15NH backbone resonances of this headpiece in the free state. Assignments of the 15N resonances of the protein were obtained in a sequential manner using heteronuclear multiple quantum coherence (HMQC), relayed HMQC nuclear Overhauser and relayed HMQC-HOHAHA spectroscopy. More than 80 per cent of residues were assigned by their 15NH(i)-N1H(i + 1) and 15NH(i)-N1H(i - 1) connectivities. Values of the 3JNH alpha splitting for 39 of the 51 residues of the headpiece were extracted from HMQC and HMQC-J. The observed 15NH(i)-C beta H cross peaks and the 3JNH alpha coupling constants values are in agreement with the three alpha-helices previously described [Zuiderweg, E.R.P., Scheek, R.M., Boelens, R., van Gunsteren, W.F. and Kaptein, R., Biochimie 67, 707 (1985)]. The 3JNH alpha coupling constants can be now used for a more confident determination of the lac repressor headpiece. From these values it is shown that the geometry of the ends of the second and third alpha-helices exhibit deviation from the canonical alpha-helix structure. On the basis of NOEs and 3JNH alpha values, the geometry of the turn of the helix-turn-helix motif is discussed.

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confidence: 99%

Two-Dimensional¹H,¹⁵N NMR investigation of uniformly¹⁵N-labeledLacRepressor Headpiece

Lancelot

Gervais

Maurizot

1992

Journal of Biomolecular Structure and Dynamics

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“…Nitrogen-35 has carbon substituents at positions a, ß, and 7, whereas N-31 has one a, two ß, and two 7 carbon substituents. Since the /3-carbon substituent effect produces a high-frequency shift of the 15N resonance and the 7 effect a smaller low frequency shift (Lichter, 1971;Pregosin et al, 1971;Sogn et al, 1973;Warren & Roberts, 1974;Gattegno et al, 1976), then N-31 is predicted to resonate to higher frequency than N-35. In the selective 15N-(*H) double resonance experiments described above, irradiation of that broad amino resonance which appeared at lower frequency resulted in decoupling of the amino l5N resonance which also appeared at lower frequency.…”

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confidence: 99%

Qualitative aspects of hydrogen-deuterium exchange in the proton, carbon-13, and nitrogen-15 nuclear magnetic resonance spectra of viomycin in aqueous solution

Hawkes¹,

Randall²,

Hull³

et al. 1978

Biochemistry

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The 1H, 13C, and 15N high field nuclear magnetic resonance spectra of the cyclic peptide viomycin have been fully assigned using homo- and heteronuclear double resonance experiments and pH effects. In addition it is shown how the two- and three-bond H-D isotope effects upon carbonyl resonances may assist in their assignment. The resistance to exchange with solvent water of the amide proton involved in the transannular hydrogen bond is observed directly in the 1H spectra, via the isotope effect on a carbonyl resonance in the 13C spectra, and via the one-bond 1H couppling in the 15N spectra.

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“…vorably with 332.0 and 347.7 ppm, respectively, which were calculated by for lysine dihydrochloride from data reported by Pregosin et al (1971).…”

Section: Resultsmentioning

confidence: 52%

Nitrogen-15 nuclear magnetic resonance of the amorphous polymer of lysine-formaldehyde-urea

Barton¹,

Himmelsbach²,

Amos³

1981

J. Agric. Food Chem.

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Natural abundance nitrogen-15 nuclear magnetic resonance spectroscopy—amino-acid derivatives

Cited by 26 publications

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Two-Dimensional¹H,¹⁵N NMR investigation of uniformly¹⁵N-labeledLacRepressor Headpiece

Two-Dimensional¹H,¹⁵N NMR investigation of uniformly¹⁵N-labeledLacRepressor Headpiece

Qualitative aspects of hydrogen-deuterium exchange in the proton, carbon-13, and nitrogen-15 nuclear magnetic resonance spectra of viomycin in aqueous solution

Nitrogen-15 nuclear magnetic resonance of the amorphous polymer of lysine-formaldehyde-urea

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Natural abundance nitrogen-15 nuclear magnetic resonance spectroscopy—amino-acid derivatives

Cited by 26 publications

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Two-Dimensional1H,15N NMR investigation of uniformly15N-labeledLacRepressor Headpiece

Two-Dimensional1H,15N NMR investigation of uniformly15N-labeledLacRepressor Headpiece

Qualitative aspects of hydrogen-deuterium exchange in the proton, carbon-13, and nitrogen-15 nuclear magnetic resonance spectra of viomycin in aqueous solution

Nitrogen-15 nuclear magnetic resonance of the amorphous polymer of lysine-formaldehyde-urea

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Two-Dimensional¹H,¹⁵N NMR investigation of uniformly¹⁵N-labeledLacRepressor Headpiece

Two-Dimensional¹H,¹⁵N NMR investigation of uniformly¹⁵N-labeledLacRepressor Headpiece