Measurement of one-bond 1Hα-13Cα couplings in backbone-labelled proteins
✍ Scribed by Alexander W. Giesen; Lynnette C. Bae; Christa L. Barrett; Jason A. Chyba; Michael M. Chaykovsky; Minn-Chang Cheng; Jenny H. Murray; Ed J. Oliver; Sarah M. Sullivan; JonathanMiles Brown; Frederick W. Dahlquist; Steve W. Homans
- Book ID
- 110299545
- Publisher
- Springer Netherlands
- Year
- 2001
- Tongue
- English
- Weight
- 95 KB
- Volume
- 19
- Category
- Article
- ISSN
- 0925-2738
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
Internal motions play an important role in the biological function of proteins and NMR relaxation studies may characterize them over a wide range of frequencies. An experimental pulse scheme is proposed for the measurement of the 13C0-13C ~ cross-relaxation rate. For sensitivity reasons, this measur
A triple-resonance pulse sequence is presented for the quantitative measurement of 1 H ␣ -13 C ␣ 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