Protein Domain PARylation Binding Efficiency Measurements

A 2026 study by Arthur Fischbach investigates noncovalent PAR binding mechanisms guiding protein PARylation. The dataset contains experimental results from a chemical biology approach using a fluorescently labeled NAD+ analogue. It compares the covalent PARylation efficiency supported by p53-CTD, RGG, WWE, PBZ, and macrodomain protein Af1521.

Use Cases

• Analyze the PARylation efficiency supported by p53-CTD, RGG, WWE, and PBZ domains versus the macrodomain protein Af1521.
• Model the relationship between noncovalent PAR binding modes and subsequent covalent modification outcomes.
• Compare the performance of intrinsically disordered regions (IDPRs) like p53-CTD and RGG against structured domains lacking IDPRs.

Strengths

• Data originates from a peer-reviewed scientific study published in 2026.
• Experimental results compare five distinct protein domains (p53-CTD, RGG, WWE, PBZ, Af1521).
• Uses a defined chemical biology approach with a fluorescently labeled NAD+ analogue.

Limitations

• Dataset is very small at 15.4 KB, indicating limited scope and likely a summary of key experimental results.
• Contains no row or column count information, limiting assessment of analytical depth.
• Focus is on specific in vitro biochemical mechanisms, not broad proteomic screening.

Provenance

Source

figshare

Collection Method

Chemical biology experiments using fluorescently labeled NAD+ analogue with defined ADP-ribose-binding domain fusion constructs.

Time Range

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Freshness

Last updated March 2026.

Geography

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