ABSTRACT
Proteins are essential for various types of cellular crosstalk. Recent advances in the area of structural biology have facilitated the deciphering of structural features of several thousand proteins. This multifaceted macromolecule is entangled in almost every cellular function. It is already well established that ~14% of proteome in archaea and bacteria and nearly 44–54% of eukaryotic proteome are enriched with disordered regions. These disordered regions are enhanced with specific amino acids that provide them flexibility in their interactions. The flexibility of intrinsic disordered regions (IDRs) augments the interaction of viral proteins with other proteins such as proteins of host immune systems. The biological properties of protein molecules are determined by the type of physical interactions that they have with other molecules. The insight that connects the sequential feature will help to determine their conformations, bimolecular assemblies, interacting partners and regulators. A comprehensive understanding will help decode the functional paradigm and folding behaviour in disease biology.
