Abstract
The folding of randomly coiled polypeptide chains into biologically active protein structures has been intensely studied for many years. In early studies by Anfinsen (1, 2), the unfolding and refolding of disulfide-rich proteins initially led to the formation of mispaired disulfide bonds (i.e., relative to the wild-type). However, in an oxidative environment, the mispaired disulfide bonds returned to their native disulfide pairings, thereby restoring normal enzyme activity. These results suggested that non-bonded interactions drive protein folding rather than the random pairing of stronger covalent disulfide bridges.
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