1H–15N correlation spectroscopy of nanocrystalline proteins
✍ Scribed by Corey R. Morcombe; Eric K. Paulson; Vadim Gaponenko; R. Andrew Byrd; Kurt W. Zilm
- Book ID
- 106401128
- Publisher
- Springer Netherlands
- Year
- 2005
- Tongue
- English
- Weight
- 758 KB
- Volume
- 31
- Category
- Article
- ISSN
- 0925-2738
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Knowledge of the magnitude and orientation of the am-is set up as a constant-time experiment in which the reference experiment is ( virtually ) free of 15 N CSA / DD relax-ide-proton chemical shift anisotropy ( CSA ) is of great interest because of its correlation with hydrogen bonding and ation int
Triple-resonance experiments capable of correlating directly bonded and proximate carbon and nitrogen backbone sites of uniformly 13 C-and 15 N-labeled peptides in stationary oriented samples are described. The pulse sequences integrate cross-polarization from 1 H to 13 C and from 13 C to 15 N with