NITROGEN-15 MAGNETIC RESONANCE SPECTROSCOPY, I. CHEMICAL SHIFTS

Nitrogen-15 Magnetic Resonance Spectroscopy. I. Chemical Shifts.

11 Felsenfeld, G., G. Sandeen, and P. von Hippel, these PROCEEDINGS, 50, 644 (1963). 12Bollum, F. J., J. Cell. Comp. Physiol., 62 (Suppi. 1), 61 (1963); Von Borstel, R. C., D. M. Prescott, and F. J. Bollum, J. Cell Biol., 19, 72A (1963). 13 Huang, R. C., and J. Bonner, these PROCEEDINGS, 48, 216 (1962); Allfrey, V. G., V. C. Littau, and A. E. Mirsky, these PROCEEDINGS, 49, 414 (1963). 14 Baxill...

Nuclear magnetic resonance spectroscopy. Ring-current effects on carbon-13 chemical shifts.

A comparison of the (13)C nuclear magnetic resonance chemical shifts of some 15,16-dialkyl-15,16-dihydropyrenes with the corresponding 15,16-dialkyl-2,7,15,16-tetrahydropyrenes provides a measure of the effect of ring current on carbon-13 chemical shifts in which other effects may be expected to be negligibly small. The general conclusion is that the absolute magnitude of the ring-current effec...

Dynamic structure of whole cells probed by nuclear Overhauser enhanced nitrogen-15 nuclear magnetic resonance spectroscopy.

The proton-decoupled 15N Fourier transform nuclear magnetic resonance (NMR) spectra of 15N-enriched Escherichia coli, Bacillus licheniformis, baker's yeast, and Friend leukemic cells were obtained. The 15N NMR spectra of whole cells displayed 15N resonances originating from (i) protein backbones with lysine, arginine, and histidine side chains, (ii) ribonucleic acids, (iii) peptidoglycan, and (...

Nitrogen-15 nuclear magnetic resonance. Structure of sulfaguanidine1.

Nitrogen-15 nuclear magnetic resonance of aliphatic tripeptides.

The 15N chemical shifts of eight aliphatic tripeptides have been measured at the natural-abundance level. For a given tripeptide, the resonances of the COOH-terminal and NH2-terminal amino acids can be identified by measurements at low or high pH. The shifts of the NH2-terminal amino acid nitrogens are essentially independent of the amino acids in the rest of the peptide. The shifts of the othe...