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- W2045610112 abstract "We describe a new experiment for measuring homonuclear-decoupled anisotropic chemical shift patterns in doubly 13C-labeled compounds under magic-angle spinning. The experiment combines a pair of selective and non-selective 180 degrees pulses to suppress the 13C-13C scalar and dipolar interactions. This is combined with the recently developed SUPER technique to recouple the chemical shift anisotropy. Demonstrations on 13Calpha and 13CO-labeled amino acids and peptides show that accurate chemical shift powder patterns can be obtained. This permits the use of chemical shift anisotropy for conformational studies of suitably extensively 13C-labeled peptides and proteins." @default.
- W2045610112 created "2016-06-24" @default.
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- W2045610112 date "2003-02-01" @default.
- W2045610112 modified "2023-09-26" @default.
- W2045610112 title "Homonuclear decoupled chemical shift anisotropy in doubly labeled peptides by selective-pulse solid-state NMR" @default.
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- W2045610112 doi "https://doi.org/10.1016/s1090-7807(02)00140-4" @default.
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