Lysozyme Aggregation Pathways from Molecular Dynamics Simulations at 300K and 340K

A molecular dynamics simulation dataset investigates the temperature-dependent aggregation mechanism of hen egg white lysozyme. The research by Shahee Islam of the University of Calcutta compares conformational changes at 300K and 340K using all-atom and coarse-grained MARTINI force field simulations. Results indicate more significant conformational changes and a more compact aggregated system at the higher temperature.

Use Cases

• Modeling protein aggregation pathways based on temperature conditions described in the study
• Comparing conformational changes in proteins based on simulation results at different temperatures
• Benchmarking coarse-grained simulation methods against all-atom models for aggregation studies
• Investigating the role of temperature in forming compact aggregated protein systems

Strengths

• Simulations conducted at two distinct temperatures (300K and 340K) for comparative analysis
• Employs both all-atom and coarse-grained (MARTINI force field) simulation methodologies
• Focuses on a specific, well-studied protein (hen egg white lysozyme) relevant to disease research

Limitations

• Column-level documentation is absent; field semantics must be inferred after download
• Row count is unknown, which may limit suitability assessment
• Last update date is unknown; freshness unverified

Provenance

Source

University of Calcutta

Collection Method

All-atom and coarse-grained molecular dynamics simulations using the MARTINI force field.