Recent structural and genomic studies have clearly shown that many proteins contain long regions that do not adopt any globular structures under native conditions. These regions are termed intrinsically disordered or unstructured, and the proteins with intrinsically disordered regions are called intrinsically disordered proteins (IDPs). Current studies estimate that one third of eukaryotic proteins contain stretches of at least 30 contiguous disordered residues, the predictions are even higher in cancer-associated and signaling proteins (80% and 67%, respectively). IDPs play crucial roles in many aspects of molecular and cell biology and numerous IDPs are associated with human diseases such as cancer, cardiovascular disease, amyloidoses, neurodegenerative diseases, diabetes and others. IDPs such as tumor suppressor P53, BRCA1, Parkinsons protein α-synuclein, Alzheimer disease protein tau and many other diseaseassociated hub proteins represent attractive targets for drugs modulating protein-protein interactions. The structures and dynamics of the disordered proteins are the basis for the novel drug discovery. IDPs are lack of stable tertiary and /or secondary structure under physiological conditions in vitro. It is difficult to obtain accurate experimental measurements for the structures and dynamics of the disordered proteins. Molecular dynamics simulations provide available powerful tools to calculate the structures and their related dynamics of IDPs. In this paper, we focus on structural and dynamics insights of disease-associated disordered proteins by molecular dynamics simulations.