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Solution structure of the thermostable sweet-tasting protein brazzein

Nature Structural Biology volume 5, pages 427431 (1998) | Download Citation

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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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Author information

Affiliations

  1. Graduate Program in Biophysics, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.

    • Jane E. Caldwell
    •  & John L. Markley
  2. Present address: Division of Hematology and Oncology, New England Medical Center, 750 Washington Street, Boston, Massachusetts 02111, USA.

    • Jane E. Caldwell
  3. Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.

    • Frits Abildgaard
    • , Željko Džakula
    •  & John L. Markley
  4. National Magnetic Resonance Facility at Madison, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.

    • Frits Abildgaard
    • , Željko Džakula
    •  & John L. Markley
  5. Department of Animal Health and Biomedical Sciences, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.

    • Ding Ming
    •  & Göran Hellekant
  6. Present address:Ingredient and Flavor Technology, Pepsi-Cola Company, Valhalla, New York 10595, USA.

    • Ding Ming

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Correspondence to John L. Markley.

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DOI

https://doi.org/10.1038/nsb0698-427

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