Specific aggregation of partially folded polypeptide chains: the molecular basis of inclusion body composition
- PMID: 9631094
- DOI: 10.1038/nbt1096-1283
Specific aggregation of partially folded polypeptide chains: the molecular basis of inclusion body composition
Abstract
During expression of many recombinant proteins, off-pathway association of partially folded intermediates into inclusion bodies competes with productive folding. A common assumption is that such aggregation reactions are nonspecific processes. The multimeric intermediates along the aggregation pathway have been identified for both the P22 tailspike and P22 coat protein. We show that for a mixture of proteins refolding in vitro, folding intermediates do not coaggregate with each other but only with themselves. This indicates that aggregation occurs by specific interaction of certain conformations of folding intermediates rather than by nonspecific coaggregation, providing a rationale for recovering relatively pure protein from the inclusion body state.
Comment in
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The specificity of protein aggregation [new; comment].Nat Biotechnol. 1996 Oct;14(10):1231. doi: 10.1038/nbt1096-1231. Nat Biotechnol. 1996. PMID: 9631084 No abstract available.
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