Mechanisms of Red-Shifted Absorption in Biliverdin-Binding Proteins

Tomoyasu Noji published a study on figshare in 2026 investigating the mechanisms of far-red and near-infrared light absorption in biliverdin-binding proteins. The dataset likely contains the results of quantum mechanical/molecular mechanical analyses used to reproduce absorption wavelengths across a broad set of proteins. The 132.5 KB text file compares the color tuning effects of chromophore conformation, electrostatic interactions, desolvation, and π-stacking between biliverdin- and phycocyanobilin-binding proteins.

Use Cases

• Training models to predict protein absorption wavelengths based on chromophore conformation and environmental factors.
• Benchmarking quantum mechanical/molecular mechanical frameworks for simulating protein-chromophore interactions.
• Analyzing the comparative effects of desolvation and π-stacking on spectral tuning in different protein families.

Strengths

• Analysis is based on a broad set of biliverdin-binding proteins studied with a consistent computational framework.
• The study quantitatively reproduces absorption wavelengths across both biliverdin- and phycocyanobilin-binding proteins.
• Specific protein examples like Agp2-PCM and sandercyanin are discussed, providing concrete cases.

Limitations

• The dataset is small at 132.5 KB, indicating limited scope.
• Row count and column-level documentation are absent; field semantics must be inferred after download.
• Description metadata is limited; actual data quality requires manual inspection after download.

Provenance

Source

figshare

Collection Method

Systematic investigation using a quantum mechanical/molecular mechanical framework.

Freshness

Last updated 2026-05-20 05:29:30; freshness should be verified.