Tissue factor (TF) contains four cysteine residues that form two disulfide bonds in the native structure of TF. Suppose TF is reduced and unfolded in urea.
If the reduced unfolded protein were oxidized prior to the removal of the urea, what fraction of the resulting mixture would you expect to possess native disulfide bonds?
Express your answer using three significant figures.
The answer is 1, i.e. the complete (100%) fraction of the resulting mixture would be expected to possess native disulfide bonds.
Explanation: When TF is reduced and unfolded in urea, both the disulfide (S-S) bonds get reduced to four thiol (SH) groups. When the reduced unfolded protein was oxidized, then the four thiol groups will be completely converted back to the two disulfide bonds as in the native state.
Tissue factor (TF) contains four cysteine residues that form two disulfide bonds in the native structure of TF. Suppose...
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