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A major question about protein folding is whether the coming together by diffusion of different segments of the polypeptide chain is rate-determining. This seemingly simple question has been very difficult to answer experimentally, but a positive result has now been obtained with one small model protein.
Background: Protein disulfide isomerase (PDI), a multifunctional protein of the endoplasmic reticulum, catalyzes the formation, breakage and rearrangement of disulfide bonds during protein folding. Dissection of this protein into its individual domains has confirmed the presence of the a and a′ domains, which are homologous to thioredoxin, having related structures and activities. The a and a′ domains...
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