Solution structure of the thermostable sweet-tasting protein brazzein

J. E. Caldwell, F. Abildgaard, Z. Dzakula, D. Ming, G. Hellekant, J. L. Markley

Research output: Contribution to journalArticlepeer-review

98 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)427-431
Number of pages5
JournalNature Structural Biology
Volume5
Issue number6
DOIs
StatePublished - Jun 20 1998

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