NMR‐monitored titration of acid‐stress bacterial chaperone HdeA reveals that Asp and Glu charge neutralization produces a loosened dimer structure in preparation for protein unfolding and chaperone activation

No abstract is available for this paper.

• Publication year

  2014

• Venue

  Protein Science

• Publication date

  2014-02-01

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1002/pro.2402PMID 24375557PMCID PMC3926742
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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