Studies on solution NMR structure of brazzein - Secondary structure and molecular scaffold

Guanghua Gao, Jixun Dai, Ming Ding, Göran Hellekant, Jinfeng Wang, Dacheng Wang

Research output: Contribution to journalArticlepeer-review

Abstract

Brazzein is a sweet-tasting protein isolated from the fruit of West African plant Pentadiplandra brazzeana Baillon. It is the smallest and the most water-soluble sweet protein discovered so far and is highly thermostable. The proton NMR study of brazzein at 600 MHz (pH 3.5, 300 K) is presented. The complete sequence specific assignments 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. A comparative analysis found that brazzein shares a so-called 'cysteine-slabilized alpha-beta' (CSαβ) motif with scorpion neurotoxins, insect defensins and plant γ-thionins. The significance of this multi-function motif, the possible active sites and the structural basis of thermostability were discussed.

Original languageEnglish (US)
Pages (from-to)417-419
Number of pages3
JournalScience in China, Series C: Life Sciences
Volume42
Issue number4
StatePublished - Aug 1 1999

Keywords

  • Brazzein
  • Proton nuclear magnetic resonance
  • Secondary structure
  • Sequential assignment
  • Sweet protein

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