Published in Proteomics Weekly, January 19th, 2004
"The three-dimensional structure of thioredoxin from Trypanosoma brucei brucei has been determined at 1.4-Angstrom resolution. The overall structure is more similar to that of human thioredoxin than to any other thioredoxin structure," researchers in Sweden, Germany, and the United States report.
"The most striking difference to other thioredoxins is the absence of a buried carboxylate behind the active site cysteines," said Rosmarie Friemann at the Swedish University of Agricultural Sciences and colleagues in the United States and Germany. "Instead...
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Source: Proteomics Weekly (2004-01-19)
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