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Protein disulfide isomerase isomerizes non-native disulfide bonds in human proinsulin independent of its peptide-binding activity
Protein disulfide isomerase (PDI) supports proinsulin folding as chaperone and isomerase. Here, we focus on how the two PDI functions influence individual steps in the complex folding process of proinsulin. We generated a PDI mutant (PDI-aba′c) where the b′ domain was partially deleted, thus abolish...
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| Hoofdauteurs: | , , , |
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| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
Wiley Subscription Services, Inc., A Wiley Company
2011
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3064837/ https://ncbi.nlm.nih.gov/pubmed/21308844 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/pro.592 |
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