Refolding of denatured trichosanthin in the presence of GroEL

Chi Kong Lau; Ricky N.S. Wong; Chun Lap Samuel Lo; Francis Kwok

doi:10.1006/bbrc.1998.8191

Refolding of denatured trichosanthin in the presence of GroEL

Chi Kong Lau, Ricky N.S. Wong, Chun Lap Samuel Lo, Francis Kwok

Research output: Journal article publication › Journal article › Academic research › peer-review

5 Citations (Scopus)

Abstract

The stability of trichosanthin (TCS), a 27-kDa ribosome-inactivating protein, was investigated in the presence of guanidinium chloride (GdnHCl). The process of unfolding was monitored by CD and fluorescence spectroscopy. Both methods show the presence of partially folded intermediates. Unfolding of TCS is attained in 6M GdnHCl, but the inactive species recover a good deal of its DNase activity upon dilution with buffer containing GroEL and ATP. The mechanism of recognition of unfolded TCS by GroEL was studied by fluorescence spectroscopy.

Original language	English
Pages (from-to)	149-154
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	245
Issue number	1
DOIs	https://doi.org/10.1006/bbrc.1998.8191
Publication status	Published - 7 Apr 1998

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1006/bbrc.1998.8191

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AU - Wong, Ricky N.S.

AU - Lo, Chun Lap Samuel

AU - Kwok, Francis

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AB - The stability of trichosanthin (TCS), a 27-kDa ribosome-inactivating protein, was investigated in the presence of guanidinium chloride (GdnHCl). The process of unfolding was monitored by CD and fluorescence spectroscopy. Both methods show the presence of partially folded intermediates. Unfolding of TCS is attained in 6M GdnHCl, but the inactive species recover a good deal of its DNase activity upon dilution with buffer containing GroEL and ATP. The mechanism of recognition of unfolded TCS by GroEL was studied by fluorescence spectroscopy.

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Refolding of denatured trichosanthin in the presence of GroEL

Abstract

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