Atomic 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.

@article{Masuda2012AtomicSO,
  title={Atomic 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.},
  author={Tetsuya Masuda and Keisuke Ohta and Bunzo Mikami and Naofumi Kitabatake and Fumito Tani},
  journal={Biochemical and biophysical research communications},
  year={2012},
  volume={419 1},
  pages={
          72-6
        }
}
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References

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High-resolution structure of the recombinant sweet-tasting protein thaumatin I.
TLDR
The high-quality structure of recombinantThaumatin with H atoms should provide details about sweetness determinants in thaumatin and provide valuable insights into the mechanism of its interaction with taste receptors.
Sweetness of Sweet Protein Thaumatin Is More Thermoresistant under Acid Conditions Than under Neutral or Alkaline Conditions
TLDR
The sweetness of thaumatin disappeared on heating at pH above 7 for 15 min, but the sweetness remained even after heating at 80°C for 4 h at pH 2.5, indicating that the sweet proteinThaumatin is more thermoresistant under acid conditions than under neutral or alkaline conditions.
High-yield Secretion of the Recombinant Sweet-Tasting Protein Thaumatin I
TLDR
Large amounts of homogeneous recombinant thaumatin allowed for preparation of high-quality crystals in the presence of cryoprotective glycerol used in high-resolution x-ray structural analysis to help further understand the perception of the sweet taste of thaumarin.
Isolation and characterization of thaumatin I and II, the sweet-tasting proteins from Thaumatococcus daniellii Benth.
TLDR
From an aqueous extract of the fruit of the tropical plant Thaumatococcus daniellii Benth, two sweet-tasting basic proteins were isolated by ultrafiltration, gel nitration on Sephadex G-50 and ion-exchange chromatography on SE-SephadeX C-25, using a sodium chloride concentration gradient.
Assignment of the disulphide bonds in the sweet-tasting protein thaumatin I.
TLDR
The disulphide linkages of the 16 half-cystine residues in the sweet-tasting protein thaumatin have been investigated by enzymatic hydrolysis of the intact molecule and the labile disulPHide bond responsible for the enzyme properties of the sweet tasting proteinThaumatin appeared to be between Cys-145 andCys-158.
Effects of pre- and pro-sequence of thaumatin on the secretion by Pichia pastoris.
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