Refolding of denatured trichosanthin in the presence of GroEL

Chi Kong Lau*, Ricky N S WONG, Samuel C.L. Lo, Francis Kwok

*Corresponding author for this work

Research output: Contribution to journalJournal articlepeer-review

5 Citations (Scopus)


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 languageEnglish
Pages (from-to)149-154
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number1
Publication statusPublished - 7 Apr 1998

Scopus Subject Areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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