A fluorescent peptide model for the thioredoxin active site

Kishore, R. ; Mathew, M. K. ; Balaram, P. (1983) A fluorescent peptide model for the thioredoxin active site FEBS Letters, 159 (1-2). pp. 221-224. ISSN 0014-5793

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/001457...

Related URL: http://dx.doi.org/10.1016/0014-5793(83)80450-5


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:Article
Source:Copyright of this article belongs to Federation of European Biochemical Societies.
Keywords:Thioredoxin Active Site; Peptide Disulfide; Fluorescent Peptide; Tryptophan Fluorescence
ID Code:4753
Deposited On:18 Oct 2010 06:50
Last Modified:16 May 2016 15:22

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