Examples
Classical examples of proteins from which the process of oxidative folding is well studied are bovine pancreatic trypsin inhibitor (BPTI) and ribonuclease A (RNaseA). These two proteins have multiple disulfide bonds and so they are very useful to follow and understand the process of oxidative folding. Another example is alkaline phosphatase, which contains two essential disulfides. It was used as an indicator protein to screen the effect of mutations in DsbA.
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