𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Three-dimensional NMR experiments for the separation of side-chain correlations in proteins via the carbonyl chemical shift

✍ Scribed by Lewis E Kay; Mitsuhiko Ikura; A.A Grey; D.R Muhandiram


Publisher
Elsevier Science
Year
1992
Weight
586 KB
Volume
99
Category
Article
ISSN
0022-2364

No coin nor oath required. For personal study only.


πŸ“œ SIMILAR VOLUMES


Two-Dimensional NMR Experiments for the
✍ Jeanine J. Prompers; Anneke Groenewegen; Cornelis W. Hilbers; Henri A.M. Peperma πŸ“‚ Article πŸ“… 1998 πŸ› Elsevier Science 🌐 English βš– 231 KB

As aromatic residues very often are part of the hydrophobic essential for an accurate and precise structure determination. core of proteins, the unambiguous assignment of the aromatic Therefore, methods for the unambiguous assignment of aroproton resonances is essential for an accurate and precise s

NMR of the methylene group: Artifacts in
✍ Alex D. Bain; Donald W. Hughes; Howard N. Hunter πŸ“‚ Article πŸ“… 1988 πŸ› John Wiley and Sons 🌐 English βš– 369 KB

When the protomproton decoupled heteronuclear two-dimensional chemical shift correlation experiment is applied to a molecule containing methylene groups, the spectra show not only the expected signals at the two proton chemical shifts, but also a strong artifact. This artifact appears at the average