| http://purl.uniprot.org/citations/22326916 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22326916 | http://www.w3.org/2000/01/rdf-schema#comment | "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 the crystal structure of thaumatin at pH 7.3 and 7.0 revealed the root-mean square deviation value of a Cα atom to be substantially greater in the large disulfide-rich region of domain II, especially residues 154-164, suggesting that a loop region in domain II to be affected by solvent conditions. Furthermore, B-factors of Lys137, Lys163, and Lys187 were significantly affected by pH change, suggesting that a striking increase in the mobility of these lysine residues, which could facilitate a reaction with a free sulfhydryl residue produced via the β-elimination of disulfide bonds by heating at a pH above 7.0. The increase in mobility of lysine residues as well as a loop region in domain II might play an important role in the heat-induced aggregation of thaumatin above pH 7.0."xsd:string |
| http://purl.uniprot.org/citations/22326916 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbrc.2012.01.129"xsd:string |
| http://purl.uniprot.org/citations/22326916 | http://purl.uniprot.org/core/author | "Masuda T."xsd:string |
| http://purl.uniprot.org/citations/22326916 | http://purl.uniprot.org/core/author | "Mikami B."xsd:string |
| http://purl.uniprot.org/citations/22326916 | http://purl.uniprot.org/core/author | "Ohta K."xsd:string |
| http://purl.uniprot.org/citations/22326916 | http://purl.uniprot.org/core/author | "Tani F."xsd:string |
| http://purl.uniprot.org/citations/22326916 | http://purl.uniprot.org/core/author | "Kitabatake N."xsd:string |
| http://purl.uniprot.org/citations/22326916 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/22326916 | http://purl.uniprot.org/core/name | "Biochem Biophys Res Commun"xsd:string |
| http://purl.uniprot.org/citations/22326916 | http://purl.uniprot.org/core/pages | "72-76"xsd:string |
| http://purl.uniprot.org/citations/22326916 | http://purl.uniprot.org/core/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."xsd:string |
| http://purl.uniprot.org/citations/22326916 | http://purl.uniprot.org/core/volume | "419"xsd:string |
| http://purl.uniprot.org/citations/22326916 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/22326916 |
| http://purl.uniprot.org/citations/22326916 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/22326916 |
| http://purl.uniprot.org/uniprot/#_P02883-mappedCitation-22326916 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/22326916 |
| http://purl.uniprot.org/uniprot/P02883 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/22326916 |