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A fluorescent peptide model for the thioredoxin active site

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.


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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
Publication: FEBS Letters
Publisher: Elsevier
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
URI: http://eprints.iisc.ac.in/id/eprint/2897

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