Kishore, R and Mathew, MK and Balaram, P (1983) A fluorescent peptide model for the thioredoxin active site. In: FEBS Letters, 159 (1-2). pp. 221-224.
A synthetic model for the active site of the protein thioredoxin has been synthesized: Boc-Trp-Cys-Gly-Pro-Cys-NHMe corresponding to residues 31-35 of the protein and possessing the 14-membered disulfide loop and a fluorescent chromophore. Dithiothreitol reduction of the disulfide bond results in a 50-60% enhancement of Trp fluorescence. The rate of reduction is solvent dependent, following the order 8 M urea >> methanol > water. The spectral changes observed in the model peptide are compared with those reported for the native protein. Circular dichroism studies suggest a substantial change in peptide backbone conformation, on disulfide reduction.
|Item Type:||Journal Article|
|Additional Information:||Copyright for this article belongs to Elsevier Science Ltd.|
|Keywords:||thioredoxin active site;peptide disulfide;fluorescent peptide;tryptophan fluorescence|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||11 Mar 2005|
|Last Modified:||19 Sep 2010 04:18|
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