Abstract
The fruit of Pentadiplandra brazzeana Baillon contains a small, sweet-tasting protein named brazzein. The structure of brazzein in solution was determined by proton nuclear magnetic resonance spectroscopy at pH 5.2 and 22 °C. The brazzein fold, which contains one α-helix and three strands of antiparallel β-sheet, does not resemble that of either of the other two sweet-tasting proteins with known structures, monellin and thaumatin. Instead, the structure of brazzein resembles those of plant γ-thionins and defensins and arthropod toxins. Sequence comparisons predict that members of a newly-identified family of serine proteinase inhibitors share the brazzein fold.
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Caldwell, J., Abildgaard, F., Džakula, Ž. et al. Solution structure of the thermostable sweet-tasting protein brazzein. Nat Struct Mol Biol 5, 427–431 (1998). https://doi.org/10.1038/nsb0698-427
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DOI: https://doi.org/10.1038/nsb0698-427
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