NMR Spectroscopic Studies of Intrinsically Disordered Proteins at Near-Physiological Conditions

摘要

Intrinsically disordered proteins (IDPs) have recently attracted the attention of the scientific community because of their peculiar features that expand our view of how protein function is determined by the conformational properties of a polypeptide chain. The discovery of numerous physiological functions performed by IDPs has challenged the traditional structure-function paradigm. The lack of a unique stable 3D structure and the high extent of local mobility provide functional advantages to IDPs in terms of structural plasticity and binding promiscuity.