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The complex role of the N-terminus and acidic residues of HdeA as pH-dependent switches in its chaperone function
HdeA is a small acid-stress chaperone protein found in the periplasm of several pathogenic gram-negative bacteria. In neutral pH environments HdeA is an inactive folded homodimer but when exposed to strong acidic environments it partially unfolds and, once activated, binds to other periplasmic prote...
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| Published in: | Biophys Chem |
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| Main Authors: | , , , , |
| Format: | Artigo |
| Language: | Inglês |
| Published: |
2020
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| Subjects: | |
| Online Access: | https://ncbi.nlm.nih.gov/pmc/articles/PMC8276670/ https://ncbi.nlm.nih.gov/pubmed/32593908 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bpc.2020.106406 |
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