Three-dimensional structure of thaumatin I, an intensely sweet protein.
- 1 March 1985
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 82 (5) , 1406-1409
- https://doi.org/10.1073/pnas.82.5.1406
Abstract
Thaumatin and monellin are the two sweetest compounds known to man--about 100,000 times sweeter than sugar on a molar basis and 3000 times on a weight basis. These proteins represent a unique class of proteins that are taste-active. We report the three-dimensional structure of thaumatin I at 3.1 A resolution.Keywords
This publication has 11 references indexed in Scilit:
- Assignment of the disulphide bonds in the sweet‐tasting protein thaumatin IEuropean Journal of Biochemistry, 1984
- Synthesis and processing of the plant protein thaumatin in yeastCell, 1984
- Cloning of cDNA encoding the sweet-tasting plant protein thaumatin and its expression in Escherichia coliGene, 1982
- The Anatomy and Taxonomy of Protein StructurePublished by Elsevier ,1981
- The toxin-agglutinin fold. A new group of small protein structures organized around a four-disulfide core.Journal of Biological Chemistry, 1980
- Methyltion of the Lysine Residues of MonellinExperimental Biology and Medicine, 1978
- Antibodies to thaumatin as a model of the sweet taste receptorNature, 1978
- Crystallization and crystal data of thaumatin I, a sweet-tasting protein fromThaumatococcus danielliibenthFEBS Letters, 1975
- Isolation and Characterization of Thaumatin I and II, the Sweet‐Tasting Proteins from Thaumatococcus daniellii BenthEuropean Journal of Biochemistry, 1972
- Design of a diffractometer and flow cell system for X-ray analysis of crystalline proteins with applications to the crystal chemistry of ribonuclease-SJournal of Molecular Biology, 1967