As nanoparticles (NPs) enter in contact with biological environments, they induce the formation of a nano-bio interface, which is the result of a complex and dynamic interaction that takes place amongst the nanomaterial surface and a variety of biomolecules, especially proteins, forming a protein corona (PC). Recently, studies of the biophysical properties of the nanoparticle protein corona (NP-PC) have become a major area of research. It is important to understand, characterise and model the biophysical properties and the molecular interactions related to the NP-PC. Understanding these properties require detailed atomistic-level studies. However, detailed molecular studies are currently lacking. In this project, we perform atomistic molecular dynamic (MD) conformational studies of proteins that are known to participate in the protein corona around the nanoparticle in the human body. Using MD-refined protein structures in conjunction with docking simulations, we generate both homo-oligomers and hetero-oligomers of corona proteins and analyse their surface biophysical properties such as their hydrophobic fraction of the solvent accessible surface area and surface charges. We also use atomistic models of TiO2 and SiO2 nanospheres, to generate and study the NP-PC interface around TiO2 and SiO2 nanoparticles. Our overarching aim is to build a multiscale framework using both atomistic and coarse-grained methods, to model and probe the detailed physiochemical properties of proteins interacting with NPs. The efficient yet accurate characterization of NP-PC biophysical properties should be useful in future studies of NP-biomolecular interactions and their possible effects (e.g., nanotoxicity) in specific biological systems.