Newcastle disease virus (NDV) is one of the paramyxovirus that has been studied at length since this virus infects the birds of all species. NDV is highly virulent in chickens and results in a high mortality rate because the V protein of NDV is found to inhibit the avian immune response system. No drugs are available for treating NDV therefore, determining the structure of V protein would help in developing a drug that can inactivate the V protein, thereby increasing the host immune response against viral infection. The research here is focused on purification and initial structural analysis of the V protein of NDV. The V protein was purified by gel filtration chromatography and the structure was studied using fluorescence and CD spectroscopy, and NMR. The results suggested that the V protein is unstructured. The research also involved purification and structural analysis of the flowering locus T (FT) protein, which is found to play a major role in theninitiation of flowering in plants. Structural analysis of the FT protein may help in finding the possible domains of the FT protein that interacts with other plant proteins, leading ton flowering. The FT protein was purified by ion exchange chromatography and the structure was studied by fluorescence and CD spectroscopy. The fluorescence data suggested that the FT protein may be folded, where as the CD data was inconclusive. More accurate secondary structure information about the protein could be obtained using NMR, but since the concentration of the FT protein was too low (0.007 mM), proper NMR study was not possible.