Crystallization and crystal data of thaumatin I, a sweet-tasting protein from Thaumatococcus daniellii benth
β Scribed by H. van der Wel; T.C. van Soest; E.C. Royers
- Book ID
- 115906052
- Publisher
- Elsevier Science
- Year
- 1975
- Tongue
- English
- Weight
- 241 KB
- Volume
- 56
- Category
- Article
- ISSN
- 0014-5793
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π SIMILAR VOLUMES
Thaumatin I has been labelled by reductive methylation of four of the E-amino groups of the lysine residues in the protein with tritiated sodium borohydride.Methy1ation with unlabelled sodium borohydride showed that up to seven amino groups can be methylated without loss of sweetness intensity. The
A two-stage procedure for the determination of a united-residue potential designed for protein simulations is outlined. In the first stage, the long-range and local-interaction energy terms of the total energy of a polypeptide chain are determined by analyzing proteinαcrystal data and averaging the