Myosin Post-translational Modifications Associated with Critical Illness Myopathy

This dataset supports a study investigating the structural and functional consequences of oxidative modifications in cardiac myosin using molecular dynamics (MD) simulations. We analyzed key oxidizable residues and their proximity to methionine, suggesting possible redox initiation points. MD trajectories of wild-type and oxidized systems (ICU_D1, ICU_D12, ICU_D12_NF) were evaluated for structural flexibility (RMSF), stability (RMSD), solvent accessibility (SASA), and inter-residue interactions. Notably, a stabilized π–cation interaction between His97 and Arg706 was observed in the non-force-generating fiber. The data includes input files, topologies, trajectories, and analysis scripts. These results provide insight into redox regulation of cardiac myosin and its potential role in impaired contractility.We update the models provided with the corresponding topologies, trajectories and analysis.