Brazzein is a sweet-tasting protein isolated from the fruit of the West African plant Pentadiplandra brazzeana Baillon. It is the smallest and the most water-soluble sweet protein discovered so far, it is also highly thermostable. The proton NMR study of brazzein at 600 MHz (pH 3.5, 300K) is presented. Complete sequence specific assignment of the individual backbone and sidechain proton resonances were achieved using through-bond and through- space connectivities obtained from standard two-dimensional NMR techniques. The secondary structure of brazzein contains one α-helix (residues 21-29), one short 310-helix (residues 14-17), two strands of antiparallel β-sheet (residues 34-39, 44-50) and probably a third strand (residues 5-7) near the N-terminus.
|Original language||English (US)|
|Number of pages||9|
|Journal||International Journal of Biological Macromolecules|
|State||Published - May 1999|
Bibliographical noteFunding Information:
The authors thank Dr Ercheng Li for assistance with NMR data collection. This work was supported by the Climb (A) Program (95-Yu-34) of the MOST of China and a special grant from the Chinese Academy of Sciences.
- Proton nuclear magnetic resonance
- Sweet protein