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Since IDPs share physicochemical characteristics that differentiate them from globular proteins, the process of IDP purification can be highly efficient if one utilizes purification schemes that take advantage of these special characteristics. However, purification can be highly problematic when dealing with recombinant IDPs that are sensitive to the degradation machinery of the host cell in which they are being overexpressed. Herein, we survey some of the specialized procedures reported in the literature for purification of IDPs, elaborate on ways to stabilize IDPs in the course of purification, and focus on our experience in the purification of two highly protease-sensitive IDPs under denaturing conditions that inactivated the endogenous proteases of the host. © 2010 John Wiley & Sons, Inc.

Original publication





Book title

Instrumental Analysis of Intrinsically Disordered Proteins: Assessing Structure and Conformation

Publication Date



695 - 704