Molecular Dynamics Simulation Studies of HYD1

The unique features of HYD1 protein and its primary involvement in fungal pathogenesis of Gibberella moniliformis have drawn attention to insilico study of potential inhibitors. This destructive mold is also on the rise of causing cancer related diseases in both humans and animals upon ingestion of the infected maize and/or rice grains. To date, currently used fungicides are ineffective against G. moniliformis as the fungus can grow and adapt to any environment. It has been realized that such behavior is attributed to class I hydrophobins where HYD1 belongs. These bio-surfactant macromolecules spontaneously self assemble at hydrophobic: hydrophilic interfaces into thin nanometric rodlet biofilms. For this reason, this paper focuses on refining a predicted HYD1 protein and studying its conformational and thermodynamic properties. Molecular dynamics simulation studies thus prove the protein to be thermally stable, compact, and results in a better quality model. This will help in understanding the self assembly mechanism of HYD1 and future docking studies.