Structural highlights
Function
[THM1_THADA] Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The intensely sweet protein thaumatin has been crystallized at 293 K in the presence of sodium tartrate and 25%(v/v) glycerol for X-ray diffraction data collection at 100 K. A comparison of the three-dimensional structure model derived from a crystal grown in the presence of glycerol with that of a control deprived of this additive reveals only minor changes in the overall structure but a approximately 20% reduction in the number of water molecules. X-ray topography analyses show that the overall quality of the crystals prepared in the presence of this cryoprotectant is enhanced.
Crystallization in the presence of glycerol displaces water molecules in the structure of thaumatin.,Charron C, Kadri A, Robert MC, Giege R, Lorber B Acta Crystallogr D Biol Crystallogr. 2002 Dec;58(Pt 12):2060-5. Epub 2002, Nov 23. PMID:12454465[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Charron C, Kadri A, Robert MC, Giege R, Lorber B. Crystallization in the presence of glycerol displaces water molecules in the structure of thaumatin. Acta Crystallogr D Biol Crystallogr. 2002 Dec;58(Pt 12):2060-5. Epub 2002, Nov 23. PMID:12454465
