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Purification of Intrinsically Disordered Proteins

  • Aviv Paz
  • , Tzviya Zeev-Ben-Mordehai
  • , Joel L. Sussman
  • , Israel Silman
  • Weizmann Institute of Science

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

6 Scopus citations

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 languageEnglish
Title of host publicationInstrumental Analysis of Intrinsically Disordered Proteins
Subtitle of host publicationAssessing Structure and Conformation
PublisherJohn Wiley and Sons
Pages695-704
Number of pages10
ISBN (Print)9780470343418
DOIs
StatePublished - 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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