This project aims to use computational structural biology approaches to investigate the molecular mechanisms governing protein–protein and protein–peptide interactions of bacterial tyrosine kinases (BY-kinases). The computational work will complement ongoing experimental studies, particularly those on enzymatic inhibition of BY-kinases, as well as investigations into their interaction networks, natural functions, and activation mechanisms. Natural activators and inhibitors will be modeled to investigate their interaction with BY-kinases and provide structural hypotheses for their mechanisms of action. Possible inhibitory peptides generated through computational approaches will be structurally modeled and evaluated through docking and, for selected complexes, MD simulations. The computational workflow will therefore combine structure analysis, molecular docking, molecular dynamics, and trajectory analysis. Computational predictions will be used to prioritize systems and interaction models for experimental investigation, while experimental results will inform the refinement and validation of computational models. High-performance computing resources are required to perform repeated MD simulations, analyze the resulting trajectories, and analyze structural datasets. Access to NAISS resources will enable simulations and computational screening to be performed with sufficient sampling and on a larger number of systems than would be feasible using local computational resources. Active storage resources are required to support the generation and analysis of MD trajectories, while completed trajectories, structural models, and associated computational data will be transferred to Chalmers institutional storage for longer-term retention.