Small angle scattering (SAS) is an important tool to study the structural properties and interactions of biological macromolecules. Numerous studies have been published about the effect of organic solvents on intramolecular protein interactions. However, little attention has been paid to the effect of organic solvents on both intra and inter molecular interactions in protein solutions. The solution behavior of major plasma proteins like human serum albumin (HSA) in the presence of methanol and glycerol was studied by small angle neutron scattering (SANS). Experiments covering a wide range of protein, salt, and cosolvent concentrations at 5, 25, and 45 °C were performed. UV and infrared spectra of selected samples were also obtained to monitor protein denaturation upon addition of the cosolvents. The radius of gyration (Rg), molecular weight and surface area were obtained by curve fitting the experimental data. The overall dimensions of HSA obtained in this work are consistent with previously reported data. Low resolution solution structures of the plasma proteins were obtained using ab initio shape reconstruction by ATSAS 2.8 package. Pairwise distribution function (P(r)) profiles were used to deduce the particle shape using GNOM. Theoretical scattering curves predicted from the models fits well with the experimental data. The models obtained closely resemble the shape of known high resolution crystallographic structures.