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Detection of key sites of dimer dissociation and unfolding initiation during activation of acid-stress chaperone HdeA at low pH
HdeA is a small acid-stress chaperone protein with a unique activity profile. At physiological pH, it forms a folded, but inactive, dimer. Below pH 3.0, HdeA unfolds and dissociates into disordered monomers, utilizing exposed hydrophobic patches to bind other unfolded proteins and prevent their irre...
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| I publikationen: | Biochim Biophys Acta Proteins Proteom |
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| Huvudupphovsmän: | , , , |
| Materialtyp: | Artigo |
| Språk: | Inglês |
| Publicerad: |
2020
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| Ämnen: | |
| Länkar: | https://ncbi.nlm.nih.gov/pmc/articles/PMC8221390/ https://ncbi.nlm.nih.gov/pubmed/33253897 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bbapap.2020.140576 |
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