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Proinsulin (a precursor to insulin) is made up of a polypeptide chain known in three parts as A, B and C. When proinsulin is converted to insulin the C part is cleaved off, leaving A and B attached only by disulfide bridges (C was in the middle of the polypeptide). In the Anfinsen experiment the beta-mercaptoethanol breaks these disulfide bridges, you now have two free, separate polypeptide chains. Thus there is no reason for them to go back together the way they originally were, just chance! It's not like a single polypeptide where the intermolecular interactions would determine how it refolded.

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Q: Why does the Anfinsen experiment not work using mature insulin?
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