ArsR Protein Arsenic Binding Affinities for Nine Homologs

Liang Cui developed a biomimetic self-assembly method to quantify arsenic binding affinities for nine ArsR protein homologs from the bacterium Rhodopseudomonas palustris CGA009. The dataset includes affinity constants and phylogenetic subgroup classifications, revealing functional diversity in arsenic-binding behavior. The data was last updated on May 22, 2026, and is shared under a CC-BY-4.0 license.

Use Cases

• Compare arsenic-binding affinities across different ArsR protein homologs based on the measured affinity constants.
• Analyze the relationship between protein structure, cysteine content, and binding affinity as described in the study.
• Evaluate the bioremediation potential of specific ArsR proteins, such as RpArsR2, for lowering arsenic accumulation in plants.
• Apply the described purification-free biomimetic platform to analyze other protein-ligand interactions.

Strengths

• Binding affinity constants are provided for nine distinct ArsR protein homologs.
• The data includes phylogenetic subgroup classifications (I, III, IV) with ranked binding affinities.
• The methodological approach is novel, using a biomimetic self-assembly platform for precise measurement.

Limitations

• The dataset is contained in a 7.1 MB DOCX file, which may require extraction of underlying data.
• Column-level documentation and sample data are unavailable, requiring manual inspection after download.
• The row count and specific data structure are unknown, limiting suitability assessment.

Provenance

Source

figshare, author Liang Cui.

Collection Method

Data generated via a novel biomimetic self-assembly approach applied to purified ArsR proteins.

Freshness

Last updated 2026-05-22 06:03:19; freshness should be verified.