A set of HNCO-based experiments for measurement of residual dipolar couplings in 15N, 13C, (2H)-labeled proteins
β Scribed by Perttu Permi; Paul R. Rosevear; Arto Annila
- Book ID
- 110263116
- Publisher
- Springer Netherlands
- Year
- 2000
- Tongue
- English
- Weight
- 165 KB
- Volume
- 17
- Category
- Article
- ISSN
- 0925-2738
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π SIMILAR VOLUMES
A triple-resonance pulse sequence is presented for the quantitative measurement of 1 H β£ -13 C β£ single-bond couplings in 15 N, 13 C uniformly labeled proteins. This 1 J CH -modulated (HACACO)NH experiment yields 1 H N -15 N-correlated 2D spectra in which the amplitude of each peak is modulated by t
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