Ck. Lau et al., REFOLDING OF DENATURED TRICHOSANTHIN IN THE PRESENCE OF GROEL, Biochemical and biophysical research communications, 245(1), 1998, pp. 149-154
The stability of trichosanthin (TCS), a 27-kDa ribosome-inactivating p
rotein, was investigated in the presence of guanidinium chloride (GdnH
Cl). The process of unfolding was monitored by CD and fluorescence spe
ctroscopy, Both methods show the presence of partially folded intermed
iates. Unfolding of TCS is attained in BM GdnHCl, but the inactive spe
cies recover a good deal of its DNase activity upon dilution with buff
er containing GroEL and ATP, The mechanism of recognition of unfolded
TCS by GroEL was studied by fluorescence spectroscopy. (C) 1998 Academ
ic Press.