Supplementary file 1_Elucidating binding hot spots and structural stability in sirtuin fam

A computational study from 2026 by Deepak Sharma, shared on figshare under a CC-BY-4.0 license, elucidates binding hot spots and structural stability in sirtuin family proteins. The 13.7 MB document details results from molecular docking and molecular dynamics simulations. It identifies isoform-selective key residues for SIRT1, SIRT2, SIRT3, SIRT5, and SIRT6 proteins.

Use Cases

• Designing selective sirtuin inhibitors based on predicted isoform-specific binding hot spots.
• Validating computational drug discovery workflows using the described molecular docking and dynamics results.
• Prioritizing target residues for experimental mutagenesis studies in sirtuin proteins.
• Comparing protein conformational dynamics across SIRT isoforms (SIRT1–7) for structural biology research.

Strengths

• Provides specific, predicted isoform-selective residues for five SIRT proteins (e.g., Phe273 for SIRT1, Phe119 for SIRT2).
• Document is 13.7 MB, suggesting detailed methodological and results documentation.
• Released under a permissive CC-BY-4.0 license for broad reuse.

Limitations

• Column-level documentation is absent; field semantics must be inferred after download.
• Row count is unknown, which may limit suitability assessment for structured data extraction.
• Data is contained in a DOCX file, which may require parsing to extract structured results.

Provenance

Source

Deepak Sharma via figshare.

Collection Method

Generated via molecular docking and molecular dynamics simulations.

Time Range

2026.

Freshness

Last updated 2026-04-10 05:57:59.

Geography

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