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Recently, various experiment methods, for example, X-ray crystallography, heteronuclear multidimensional NMR, Far UV CD and gel filtration, characterized “natively unfolded” or “intrinsic disorder” regions in many proteins. These phenomena in the physiological condition are common. In spite of lacking folded structure, it is apparent that they play fundamental roles in biological activities.
It is suggested that disorder regions serve fundamental roles in biological activities. For instance, they are involved in signaling, cell cycle control and molecular recognition. They are also associated with diseases that are mediated by protein misfolding and aggregation. So, they are important for understanding protein function.
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