Solution conformation of brazzein by 1H nuclear magnetic resonance: Resonance assignment and secondary structure

Guang Hua Gao, Ji Xun Dai, Ming Ding, Göran Hellekant, Jin Fen Wang, Da Cheng Wang

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


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 languageEnglish (US)
Pages (from-to)351-359
Number of pages9
JournalInternational Journal of Biological Macromolecules
Issue number4
StatePublished - May 1 1999


  • Brazzein
  • Proton nuclear magnetic resonance
  • Sweet protein

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