Transient Helicity Measurements in ACTR Protein Variants via Hydrogen Exchange

Hydrogen exchange data for four variants of the intrinsically disordered protein ACTR activation domain, differing in helical propensity. The dataset includes NMR-based exchange rates and pseudo-protection factors referenced to the wild-type protein. It was created by I. Simina Cuciurean and published on figshare in April 2026.

Use Cases

• Compare pseudo-protection factors across four ACTR protein variants to assess differences in transient helicity.
• Correlate hydrogen exchange-derived pseudo-protection factors with helicity measurements from NMR chemical shifts.
• Validate the sensitivity of hydrogen exchange for detecting subtle structural differences in highly dynamic protein regions.
• Benchmark hydrogen exchange as a complementary method to NMR chemical shift analysis for characterizing IDP structure.

Strengths

• Data for four distinct protein variants enables comparative analysis of helical propensity.
• Pseudo-protection factors are calculated to enable robust comparison without relying on intrinsic peptide-based rates.

Limitations

• The dataset is small, with a file size of 400.0 KB, indicating limited scope and likely low row count.
• The analysis is specific to the ACTR protein domain, limiting generalizability to other IDP systems without further validation.

Provenance

Source

figshare, authored by I. Simina Cuciurean.

Collection Method

Hydrogen exchange measured by NMR and mass spectrometry (HDX-MS) on synthesized protein variants.

Freshness

Last updated in April 2026, indicating recent data.