Spectrometric Investigation of Thaumatin I and II, Two Sweet-Tasting Proteins from Thaumatococcus daniellii Benth

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The relationship between thaumatin, a sweet protein and thaumatopain, a cysteine protease, from the arlis of Thaumatococcus daniellii.

Thaumatin, an intensely sweet protein, is the major proteinaciouscompnentinthe arils ofThaumatococcusdaniellii [l].Thaumatinisamemberofafamilyofatleastfiveisoforms, separable on cation exchange chromatography and all with a molecular weight of approx. 22 kDa and possessing eight disulphide bridges. Thaumatin I and II are derived from distinct genes, the other subforms may result from post-trans...

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Crystal structure of the sweet-tasting protein thaumatin II at 1.27Å.

Thaumatin, an intensely sweet-tasting protein, elicits a sweet taste sensation at 50 nM. Here the X-ray crystallographic structure of one of its variants, thaumatin II, was determined at a resolution of 1.27 Å. Overall structure of thaumatin II is similar to thaumatin I, but a slight shift of the Cα atom of G96 in thaumatin II was observed. Furthermore, the side chain of residue 67 in thaumatin...

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High-resolution structure of the recombinant sweet-tasting protein thaumatin I.

Thaumatin, an intensely sweet-tasting plant protein, elicits a sweet taste at a concentration of 50 nM. The crystal structure of a recombinant form of thaumatin I produced in the yeast Pichia pastoris has been determined to a resolution of 1.1 Å. The model was refined with anisotropic B parameters and riding H atoms. A comparison of the diffraction data and refinement statistics for recombinant...

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Rhinitis induced to mace

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ژورنال

عنوان ژورنال: European Journal of Biochemistry

سال: 1973

ISSN: 0014-2956,1432-1033

DOI: 10.1111/j.1432-1033.1973.tb02872.x