Insulin-like growth factor (IGF-1) contains three
disulfide bonds. In the presence of denaturant and thiol
catalyst, IGF-1 shuffles its native disulfide bonds and
denatures to form a mixture of scrambled isomers. The composition
of scrambled IGF varies under different denaturing conditions.
Among the 14 possible scrambled IGF isomers, the yield
of the beads-form isomer is shown to be directly proportional
to the strength of the denaturing condition. This paper
demonstrates a new approach to quantify the extent of unfolding
of the denatured protein.
