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The structure of HdeB. (a) The structure of HdeB (cyan) superimposed ...

The Chaperone-Active State of HdeB at pH 4 Arises from Its ...

A model for E. coli HdeB chaperone mechanism.: (A) A schematic ...

Formation of Fibrils by the Periplasmic Molecular Chaperone HdeB from ...

Formation of Fibrils by the Periplasmic Molecular Chaperone HdeB from ...

The Chaperone-Active State of HdeB at pH 4 Arises from Its ...

The structure of HdeB. (a) The structure of HdeB (cyan) superimposed ...

H-dependent conformational changes of E. coli HdeB characterized by ...

HdeB Functions as an Acid-protective Chaperone in Bacteria* - Journal ...

Evolutionary Silence of the Acid Chaperone Protein HdeB in ...

Formation of Fibrils by the Periplasmic Molecular Chaperone HdeB from ...

Complex formation of HdeB dimers with unfolded LDH at pH 4 by ...

ANS fluorescence of HdeB and HdeA at neutral and acidic pHs. The ...

Complex formation of HdeB dimers with unfolded LDH at pH 4 by ...

HdeB Functions as an Acid-protective Chaperone in Bacteria* - Journal ...

Substrate-dependent HdeA and HdeB aggregation. Increasing amounts of ...

HdeB Functions as an Acid-protective Chaperone in Bacteria* - Journal ...

Figure S1: Size exclusion chromatography of HdeA and HdeB at pH 7 ...

Substrate-dependent HdeA and HdeB aggregation. Increasing amounts of ...

ANS fluorescence of HdeB and HdeA at neutral and acidic pHs. The ...

Contribution of HdeA and HdeB to acid resistance of E. coli strains ...

Model-free ananysis of E. coli HdeB backbone dynamics at neutral and ...

E. coli lacking HdeA and HdeB are more sensitive to acid shock and ...

Evolutionary Silence of the Acid Chaperone Protein HdeB in ...

Contribution of HdeA and HdeB to acid resistance of E. coli strains ...

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HdeB Functions as an Acid-protective Chaperone in Bacteria* - Journal ...

Evolutionary Silence of the Acid Chaperone Protein HdeB in ...

Formation of Fibrils by the Periplasmic Molecular Chaperone HdeB from ...

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Formation of Fibrils by the Periplasmic Molecular Chaperone HdeB from ...

Formation of Fibrils by the Periplasmic Molecular Chaperone HdeB from ...

Formation of Fibrils by the Periplasmic Molecular Chaperone HdeB from ...

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Formation of Fibrils by the Periplasmic Molecular Chaperone HdeB from ...

HdeB chaperone activity is coupled to its intrinsic dynamic properties ...

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(PDF) HdeB Functions as an Acid-Protective Chaperone in Bacteria.

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Sequence and structural comparison between HdeA and HdeB. (A) Protein ...

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Solution structures of E. coli HdeB.: (A,B) 20 lowest-energy structure ...

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Detection of the pH-dependent Activity of Escherichia coli Chaperone ...

Sequence and structural comparison between HdeA and HdeB. (A) Protein ...

The internal salt bridges within HdeB. (a) In each monomer, a salt ...

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Solubilization of Protein Aggregates by the Acid Stress Chaperones HdeA ...

Solubilization of Protein Aggregates by the Acid Stress Chaperones HdeA ...

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Sequence and structural comparison between HdeA and HdeB. (A) Protein ...

Solution structures of E. coli HdeB.: (A,B) 20 lowest-energy structure ...

Solubilization of Protein Aggregates by the Acid Stress Chaperones HdeA ...

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Micro- to milli-second timescale conformational exchanges of E. coli ...

Schematic illustration of the results described in the present study ...

Solubilization of Protein Aggregates by the Acid Stress Chaperones HdeA ...

Sequence and structural comparison between HdeA and HdeB. (A) Protein ...

Comparative proteomics reveal distinct chaperone–client interactions in ...

Detection of the pH-dependent Activity of Escherichia coli Chaperone ...

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Solution structures of E. coli HdeB.: (A,B) 20 lowest-energy structure ...

Detection of the pH-dependent Activity of Escherichia coli Chaperone ...

Sequence and structural comparison between HdeA and HdeB. (A) Protein ...

Detection of the pH-dependent Activity of Escherichia coli Chaperone ...

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Size of protein aggregates. Periplasmic extracts from the hdeA mutant ...

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Solution structures of E. coli HdeB.: (A,B) 20 lowest-energy structure ...

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Comparative proteomics reveal distinct chaperone–client interactions in ...

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Comparative proteomics reveal distinct chaperone–client interactions in ...

Cell membrane alteration of acid-tolerant bacteria to acid stress. a ...

| An overview of the molecular chaperones in the periplasm of E. coli ...

Comparative proteomics reveal distinct chaperone–client interactions in ...

Size of protein aggregates. Periplasmic extracts from the hdeA mutant ...

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Schematic illustration of the results described in the present study ...

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Stress-Responsive Periplasmic Chaperones in Bacteria - PMC

bis-ANS labeling. Periplasmic extracts from the hdeA mutant (20 ␮ g ...