Solution conformation of brazzein by 1H nuclear magnetic resonance: resonance assignment and secondary structure.
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 alpha-helix (residues 21-29), one short 3(10)-helix (residues 14-17), two strands of antiparallel beta-sheet (residues 34-39, 44-50) and probably a third strand (residues 5-7) near the N-terminus.
Gao
G H
GH
Department of Protein Engineering, Institute of Biophysics, Chinese Academy of Sciences, Beijing, People's Republic of China.
Dai
J X
JX
Ding
M
M
Hellekant
G
G
Wang
J F
JF
Wang
D C
DC
D000595:Amino Acid Sequence; D004220:Disulfides / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid; D012996:Solutions / Q000737:chemistry
D004220:Disulfides; D010940:Plant Proteins; D012996:Solutions; C090521:brazzein protein, Pentadiplandra brazzeana