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Unfolded DapA forms aggregates when diluted into free solution, confounding comparison with folding by the GroEL/GroES chaperonin system
A recent hydrogen-deuterium exchange study of folding of the GroEL/GroES-dependent bacterial enzyme DapA has suggested that the DapA folding pathway when free in solution may differ from the folding pathway used in the presence of the GroEL/GroES chaperonin. Here, we have investigated whether DapA a...
Αποθηκεύτηκε σε:
| Τόπος έκδοσης: | FEBS Lett |
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| Κύριοι συγγραφείς: | , , , , |
| Μορφή: | Artigo |
| Γλώσσα: | Inglês |
| Έκδοση: |
2015
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| Θέματα: | |
| Διαθέσιμο Online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4410871/ https://ncbi.nlm.nih.gov/pubmed/25601566 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.febslet.2015.01.008 |
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