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 present...

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Bibliographic Details
Published in:International journal of biological macromolecules 1999-05, Vol.24 (4), p.351-359
Main Authors: Gao, Guang-Hua, Dai, Ji-Xun, Ding, Ming, Hellekant, Göran, Wang, Jin-Fen, Wang, Da-Cheng
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Brazzein
Disulfides - chemistry
Magnetic Resonance Spectroscopy
Models, Molecular
Molecular Sequence Data
Plant Proteins - chemistry
Protein Conformation
Protein Structure, Secondary
Proton nuclear magnetic resonance
Sequence Homology, Amino Acid
Solutions - chemistry
Sweet protein
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Summary: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 3 10-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.
ISSN:0141-8130
1879-0003
DOI:10.1016/S0141-8130(99)00055-0