𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Support of1H NMR assignments in proteins by biosynthetically directed fractional13C-labeling

✍ Scribed by Thomas Szyperski; Dario Neri; Barbara Leiting; Gottfried Otting; Kurt Wüthrich


Publisher
Springer Netherlands
Year
1992
Tongue
English
Weight
742 KB
Volume
2
Category
Article
ISSN
0925-2738

No coin nor oath required. For personal study only.


📜 SIMILAR VOLUMES


An1H–13C–13C-Edited1H NMR Experiment for
✍ Feng Qiu; Mario Rivera; Ruth E. Stark 📂 Article 📅 1998 🏛 Elsevier Science 🌐 English ⚖ 159 KB

In paramagnetic heme proteins, it is often problematic to make the reduced (usually diamagnetic) state lack isotropic shifts proton resonance assignments for heme substituents that do not and are therefore difficult to examine by NMR spectroscopy. have large isotropic shifts and consequently lie und

Unequivocal assignment of the position o
✍ P. D. Stanley; R. J. Cremlyn; J. Nangle; F. J. Swinbourne 📂 Article 📅 1988 🏛 John Wiley and Sons 🌐 English ⚖ 265 KB

The 'H and 13C NMR spectra of a sulphamoyl derivative of DL-camphor have been examined. The unequivocal assignment of the position of substitution has been achieved by the attached proton test, 2D correlation spectroscopy and NOE difference spectroscopy.

Sequential assignment of 1H, 15N, 13C re
✍ Hong Qian; Michael S. Rogers; Jürgen Schleucher; Ulf Edlund; Emanuel E. Strehler 📂 Article 📅 1998 🏛 Cold Spring Harbor Laboratory Press 🌐 English ⚖ 884 KB

## Abstract Human calmodulin‐like protein (CLP) is closely related to vertebrate calmodulin, yet its unique cell specific expression pattern, overlapping but divergent biochemical properties, and specific target proteins suggest that it is not an isoform of calmodulin. To gain insight into the stru