The interferon-induced transmembrane protein (IFITM) family, including IFITM1, IFITM2, and IFITM3, constitutes a vital component of the CD225 superfamily and plays a crucial role in defending against various viruses by hindering their entry into cells. Unlike mechanisms relying on specific viral recognition, IFITM proteins alter the mechanical properties of cellular membranes, increasing rigidity and decreasing fluidity, thereby preventing the fusion of viral and cellular membranes. Specifically, IFITM3 has been studied in detail, revealing key structural features that contribute to its activity. The topology of IFITM3 in micelles reveals two short intramembrane α-helices within a hydrophobic region, likely inducing membrane curvature when inserted into a single leaflet of the lipid bilayer. Notably, the amphipathic helix (AH) has been identified as essential for the antiviral activity, responsible for altering membrane properties, such as reducing flexibility. However, the precise molecular mechanism remains unclear. This proposal aims to investigate the structural properties of IFITM proteins at the molecular level by employing coarse-grained and atomistic molecular dynamics simulations to explore the conformational changes of proteins and their dynamic interactions within the lipid environment. This exploration intends to shed light on how such interactions impact membrane properties. We respectfully request allocation of CPU and GPU computing resources on the Dardel supercomputer to advance our academic research. For analysis purposes, we will apply machine learning which requires access to Alvis computing resources.