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Oxidative folding intermediates with nonnative disulfide bridges between adjacent cysteine residues
The oxidative folding of the Amaranthus α-amylase inhibitor, a 32-residue cystine-knot protein with three disulfide bridges, was studied in vitro in terms of the disulfide content of the intermediate species. A nonnative vicinal disulfide bridge between cysteine residues 17 and 18 was found in three...
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| Autori principali: | , , , , , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
The National Academy of Sciences
2003
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC156273/ https://ncbi.nlm.nih.gov/pubmed/12724517 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.2225470100 |
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