Intrinsically Disordered Proteins (IDPs) are active in different cellular procedures like
ordered assembly of chromatin and ribosomes, interaction with membrane, protein, and ligand
binding, molecular recognition, binding, and transportation via nuclear pores, microfilaments and
microtubules process and disassembly, protein functions, RNA chaperone, and nucleic acid binding,
modulation of the central dogma, cell cycle, and other cellular activities, post-translational
qualification and substitute splicing, and flexible entropic linker and management of signaling
pathways. The intrinsic disorder is a precise structural characteristic that permits IDPs/IDPRs to
be involved in both one-to-many and many-to-one signaling. IDPs/IDPRs also exert some dynamical
and structural ordering, being much less constrained in their activities than folded proteins. Nuclear
magnetic resonance (NMR) spectroscopy is a major technique for the characterization of
IDPs, and it can be used for dynamic and structural studies of IDPs. This review was carried out
to discuss intrinsically disordered proteins and their different goals, as well as the importance and
effectiveness of NMR in characterizing intrinsically disordered proteins in healthy and diseased
states.