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Real-time and equilibrium (19)F-NMR studies reveal the role of domain–domain interactions in the folding of the chaperone PapD
PapD is a periplasmic chaperone essential for P pilus formation in pyelonephritic strains of E. coli. It is composed of two domains, each of which contains a tryptophan residue (Trp-36 and Trp-128, in the N- and C-terminal domains, respectively). To explore the role of domain–domain interactions dur...
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| Main Authors: | , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
The National Academy of Sciences
2002
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC117370/ https://ncbi.nlm.nih.gov/pubmed/11792867 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.022649599 |
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