Ghoshal, Alokesh K (1999) Minithioredoxin: A Folded and Functional Peptide Fragment of Thioredoxin. In: Biochemical and Biophysical Research Communications, 261 (3). pp. 676-681.
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A peptide fragment comprising the first 83 residues from the N-terminus of E. coli thioredoxin is purified by hydroxylamine cleavage of the intact protein. At physiological pH, the secondary and tertiary structure contents of the peptide are 70 and 35%, respectively, compared to the intact protein. Peptide 83 is able to display dual biological functions of thioredoxin, namely, a substrate for the enzyme E. coli thioredoxin-reductase and a processivity factor of T7 DNA polymerase. At present, peptide 83 represents the minimum functional and folding unit of thioredoxin. The highly conserved residue Phe 81 appears to play an important role in the folding of peptide 83, as judged from the packing analysis. Peptide 83 also mimics a particular kinetic folding intermediate of thioredoxin in terms of spectral properties and may serve as an equilibrium peptide model for the former.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Elsevier.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||09 Oct 2007|
|Last Modified:||19 Sep 2010 04:40|
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