Assignment of the disulphide bonds in the sweet-tasting protein thaumatin I
نویسندگان
چکیده
منابع مشابه
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...
متن کاملCrystal 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...
متن کاملProtein disulphide-isomerase and the formation of native disulphide bonds.
Disulphide bonds are found in practically every class of extracellular protein, and the formation of disulphide bonds must be regarded as a key post-translational modification of secretory proteins. Despite this, and despite the fact that the existence of disulphide bonds has been known for many years, the mechanism of disulphide bond formation during protein biosynthesis and secretion is not w...
متن کاملAtomic structure of the sweet-tasting protein thaumatin I at pH 8.0 reveals the large disulfide-rich region in domain II to be sensitive to a pH change.
Thaumatin, an intensely sweet-tasting plant protein, elicits a sweet taste at 50 nM. Although the sweetness remains when thaumatin is heated at 80 °C for 4h under acid conditions, it rapidly declines when heating at a pH above 6.5. To clarify the structural difference at high pH, the atomic structure of a recombinant thaumatin I at pH 8.0 was determined at a resolution of 1.0Å. Comparison to th...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1984
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1984.tb08428.x