In its fully extended form, three billion base pair long DNA polymer of human genome is about two meter long. Yet, it is contained in the nucleus of the cell having an average size of about 10 um. This much complex packaging is done with the help of highly basic proteins called Histones which forms the nucleosome. Although DNA is very tightly compacted, it nevertheless remain accessible to the many enzyme machinery that replicates it, repairs it and use its genes to produce RNA molecules and proteins. For access to genomic DNA by proteins controlling and expressing the genome, the nucleosome must be remodeled, and such remodeling must include unwrapping of DNA from the nucleosome core. The highly intrinsically disordered and positively charged Nterminal tails of the histone proteins play a central role in this process. Although the structure of the nucleosome core particle has been determined by X-ray crystallography at near-atomic resolution, the histone tails are not observed in this structure. Knowing the structure and dynamics of these tails and their role in nucleosome architecture will help us to understand the regulation of gene expression. Intrinsically disordered histone tails might be able to change their conformation easily upon binding to other proteins or DNA, providing a framework to explain their multiple and complex roles. Since X-ray crystallography and cryo-EM are not able to capture these disordered tails, we are employing sophisticated NMR techniques to elucidate their structure and dynamics.