Abstract: Three organic solubilization techniques were developed for a vaccine analogue, bacteriophage MS2: dry solubilization (DS), reverse micelle solubilization (RM) and 'azeodried' solubilization (AZ). The surfactant Aerosol OT (AOT) was used in each case to solubilize the naked virus in organic solvent. For each solubilization technique, the amount of AOT and isooctane remained the same, while the amount of water solubilized in each formulation varied. The solubilization efficiency of each formulation was compared: DS (5%), RM (67%) and AZ (47%). The viability of the solubilized samples were tested and found to contain virus that could replicate. Further, the RM and AZ formulations of MS2 were found to be stable after heating to 90°C for twenty minutes while DS, aqueous and N2-dried samples of MS2 were not. The utility of MS2 solubilization in organic solvent was demonstrated through a bioconjugation that was impossible to perform in aqueous solution. In order to show the compatibility of the solubilization techniques with other biological substrates, hemoglobin was solubilized using a similar procedure. Hemoglobin, an important blood protein of commercial interest, allowed for the facile determination of thermal or solvent induced unfolding by loss of the absorbance of the bound heme in the active site of the protein. The protein was found to resist heat treatment at 90°C for twenty minutes in a polystyrene matrix. Organic solvent solubilization alone increased the melt temperature of the protein from 43°C (for aqueous buffer) to 76°C (AZ in isooctane), as measured by dynamic light scattering. Tobacco mosaic virus (TMV) is a rod-shaped virus, 17 ran in diameter and 300 nm in length. TMV is an important target as a scaffold for nanometer-scaled advanced materials such as a synthetic light harvesting system. The solubilization of the relatively large TMV demonstrated that the solubilization procedure could be generalized to other viruses. Dynamic light scattering was employed to measure the effective diameter of the solubilized species. The virus was found to be two orders of magnitude larger than the protein-free reverse micelle system alone, suggesting that the virus was aggregated in the organic solvent. However, the presence of a non-zero rotational diffusion coefficient suggested that the solution of solubilized virus aggregates contains rod-like scattering moieties.