ProOmpA contains secondary and tertiary structure prior to translocation and is shielded from aggregation by association with SecB protein.

Escherichia coli protein export involves cytosolic components termed molecular chaperones which function to stabilize precursors for membrane translocation. It has been suggested that chaperones maintain precursor proteins in a loosely folded state. We now demonstrate that purified proOmpA in its tr...

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Detaylı Bibliyografya
Asıl Yazarlar: Lecker, S H, Driessen, A J, Wickner, W
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: 1990
Konular:
Research Article
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC551957/
https://ncbi.nlm.nih.gov/pubmed/2192862
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