Intrinsically disordered proteins (IDPs) are a class of proteins that lacks an unique three dimensional structure and form a heterogeneous ensemble of configurations. In recent times, IDPs draw significant attention because of their diverse roles in cell signaling, gene regulation, etc through compartmentalizing the biomolecules in cells. But, maturation of the compartmentalized condensed phase can lead to the aggregation of protein molecules, which can cause a number of neurodegenerative diseases such as Alzheimer, Perkinson, and Huntington. Characterization of IDPs at the molecular level is therefore crucial in identifying their aberrant and functional behaviour. In addition, internal factors such as chain length, composition of amino acid residues, and their arrangement in primary sequence, and, external factors such as temperature, pH, salts, and cosolvents can affect the conformations of IDPs significantly. I have developed a coarse grained model for the IDPs and I am interested to study various aspects of IDPs in the presence of cosolvents and salts using the techniques of molecular dynamics simulations and tools of statistical thermodynamics.