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- W2358934435 abstract "Objective: The stability and kinetics of self-assembled complex may be effected by the size, charge and polarity of a residue in a α/β domain. Methods: We choose L79Y mutant of thioredoxin in which at position 79 leucine is substituted by tyrosine. In this mutant, the residue's polarity is stronger than wild type TRX. After we compared the stability of the complex of the re-assembled N fragment and C fragment of wild type TRX with the complex of the re-assembled N fragment and C fragment of L79Y mutant and the kinetics of these two complexes. Results: (1) The stability of re-assembled complex which N fragment (1-73) combines with C fragment from L79Y is much more unstable than the complex from the wild type thioredoxin. (2) The kinetics of the re-assembly complex of the L79Y is different from that of wild type thioredoxin. Conclusion: The rate constant of the re-assembly of the L79Y mutant's N fragment and C fragment is much higher than that of the wild type thioredoxin.;" @default.
- W2358934435 created "2016-06-24" @default.
- W2358934435 creator A5013273035 @default.
- W2358934435 date "2002-01-01" @default.
- W2358934435 modified "2023-09-22" @default.
- W2358934435 title "COMPARISON OF THE STABILITY AND KINETICS OF THE SELF-ASSEMBLED THIOREDOXIN FRAGMENTS WITH IT'S L79Y MUTANT" @default.
- W2358934435 hasPublicationYear "2002" @default.
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