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Identification of residual structure within denatured antichymotrypsin: implications for serpin folding and misfolding

Pearce, Mary C., Cabrita, Lisa D., Rubin, Harvey, Gore, Michael G. and Bottomley, Stephen P. (2004) Identification of residual structure within denatured antichymotrypsin: implications for serpin folding and misfolding Biochemical and Biophysical Research Communications, 324, (2), pp. 729-735. (doi:10.1016/j.bbrc.2004.09.105).

Record type: Article


The native serpin fold is metastable and possesses the inherent ability to convert into more stable, but inactive, conformations. In order to understand why serpins attain the native fold instead of other more thermodynamically favourable folds we have investigated the presence of residual structure within denatured antichymotrypsin (ACT). Through mutagenesis we created a single tryptophan variant of ACT in which a Trp residue (276) is situated on the H-helix, located within a region known as the B/C barrel. The presence of residual structure around Trp 276 in 5 M guanidine hydrochloride (GdnHCl) was shown by fluorescence and circular dichroism spectroscopy and fluorescence lifetime experiments. The residual structure was disrupted in the presence of 5 M guanidine thiocyanate (GdnSCN). Protein refolding studies showed that significant refolding could be achieved from the GdnHCl denatured state but not the GdnSCN denatured form. The implications of these data on the folding and misfolding of the serpin superfamily are discussed.

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Published date: 12 November 2004
Keywords: serpin, conformational disease, protein misfolding, residual structure, aggregation, antichymotrypsin, antitrypsin, protein folding


Local EPrints ID: 56509
ISSN: 0006-291X
PURE UUID: bfe97814-cba5-42e9-9c0f-6dce4f0b9a3c

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Date deposited: 07 Aug 2008
Last modified: 17 Jul 2017 14:30

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Author: Mary C. Pearce
Author: Lisa D. Cabrita
Author: Harvey Rubin
Author: Michael G. Gore
Author: Stephen P. Bottomley

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