Supplementary file 1_An In silico analysis on the phosphorylation dependent structural and

A 113.0 KB DOCX file contains supplementary data and analysis from an in silico study on protein thermostability. The research by Sermarajan Arunachalam, last updated in May 2026, investigates the effect of phosphorylation on two thermophilic proteins, 1QMP and 1DZ3, using molecular dynamics simulations. The file likely contains results from root-mean-square deviation, root-mean-square fluctuation, and vibrational energy transfer calculations.

Use Cases

• Analyzing structural rigidity and flexibility based on root-mean-square deviation and fluctuation data mentioned in the description
• Studying intramolecular energy propagation pathways based on vibrational energy transfer calculations described in the study
• Comparing thermal resistance and unfolding mechanisms between phosphorylated and non-phosphorylated protein models based on steered molecular dynamics simulations
• Visualizing key residue interaction networks for energy transport based on the communication maps referenced in the description

Strengths

• File size is precisely 113.0 KB, indicating a focused supplementary document.
• The study provides a direct comparison between two specific protein structures (1QMP and 1DZ3) with and without phosphorylation.
• Analysis is based on established computational methods like molecular dynamics, RMSD, and RMSF.

Limitations

• Row count and column-level documentation are absent; field semantics must be inferred after download.
• The dataset is a single 113.0 KB DOCX file, which suggests a very limited scope and likely contains summarized results rather than raw simulation data.
• Description metadata is limited; actual data quality and structure require manual inspection after download.

Provenance

Source

figshare

Collection Method

Data likely generated from molecular dynamics simulations performed in the described study.

Freshness

Last updated 2026-05-06 10:52:48; freshness should be verified.