A novel experiment for the quantitative measurement of CSA(1HN)/CSA(15N) cross-correlated relaxation in 15N-labeled proteins*
โ Scribed by Marco Tessari; Geerten W. Vuister
- Book ID
- 110262577
- Publisher
- Springer Netherlands
- Year
- 2000
- Tongue
- English
- Weight
- 65 KB
- Volume
- 16
- Category
- Article
- ISSN
- 0925-2738
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๐ SIMILAR VOLUMES
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
We present a simple method for extracting interference effects between chemical shift anisotropy (CSA) and dipolar coupling from spin relaxation measurements in macromolecules, and we apply this method to extracting cross-correlation rates involving interference of amide 15N CSA and 15N-1H dipolar c
Very precise measurements of 1 J NH couplings have been made J-resolved experiment, the selective-coupling-enhanced for approximately 40% of the amide sites in cyanometmyoglobin HSQC (SCE-HSQC) experiment, which allows one-bond using two different experimental approaches. The first approach amide co