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

Biochemical and Biophysical Research Communications

Volumn 419, Issue 1, 2012, Pages 72-76

  Masuda, Tetsuya ^a   Ohta, Keisuke ^a   Mikami, Bunzo ^a   Kitabatake, Naofumi ^b   Tani, Fumito ^a  

^a KYOTO UNIVERSITY   (Japan)

^b NOTRE DAME SEISHIN UNIVERSITY   (Japan)

Author keywords

Alkaline conditions; Heat; Hydrogen atoms; SHELXL; Sweet tasting protein; Thaumatin

Indexed keywords

LYSINE; SOLVENT; THAUMATIN; THAUMATIN I; THIOL DERIVATIVE; UNCLASSIFIED DRUG;

ALKALINITY; ARTICLE; ATOM; CHEMICAL REACTION; CRYSTAL STRUCTURE; DISULFIDE BOND; HEATING; PH; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DOMAIN;

HYDROGEN-ION CONCENTRATION; MODELS, CHEMICAL; PLANT PROTEINS; PROTEIN STRUCTURE, TERTIARY; SWEETENING AGENTS; TASTE;

EID: 84857655224     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.01.129     Document Type: Article

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