Abstract
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.
| Original language | English |
|---|---|
| Title of host publication | Instrumental Analysis of Intrinsically Disordered Proteins |
| Subtitle of host publication | Assessing Structure and Conformation |
| Publisher | John Wiley and Sons |
| Pages | 695-704 |
| Number of pages | 10 |
| ISBN (Print) | 9780470343418 |
| DOIs | |
| State | Published - Sep 9 2010 |
Keywords
- Intrinsically disordered protein purification
- Purification under denaturing conditions-for bovine viral diarrhea virus core protein, an IDP
- Purification using thermal denaturation
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