Scientists at Michigan Technological University want to manipulate and better understand the surface proteins of Porcine Parvovirus. In vaccine purification the interaction between the virus and the surrounding heterogeneous mixture are important to the effectiveness of the vaccine. If the viral components fall apart then the mixture cannot be used as a therapeutic. Also the viruses’ surfaces contain many co receptors that are important for cell recognition and replication in a host. The main finding of the paper was improving the computational methods of viral surface chemistry as compared to the experimental calculations. The researchers compared the hydrophobicity of PPV to the to other studied models of viral proteins that can repel and attract water. They focused on the most accessible area of the PPV virus known as the solvent accessible surface area. As the viral capsid was too large to look at all the capsid proteins they focused on VP2, the most abundant one. The strong correlation between experimental and computational results shows that PPV like other viruses have a measurable hydrophobicity. This may lead to better techniques to catch viruses or purify them.