A Novel Tandem-Tag Purification Strategy for Challenging Disordered Proteins.

ABSTRACT: Intrinsically disordered proteins (IDPs) lack well-defined 3D structures and can only be described as ensembles of different conformations. This high degree of flexibility allows them to interact promiscuously and makes them capable of fulfilling unique and versatile regulatory roles in cellular processes. These functional benefits make IDPs widespread in nature, existing in every living organism from bacteria and fungi to plants and animals. Due to their open and exposed structural state, IDPs are much more prone to proteolytic degradation than their globular counterparts. Therefore, the purification of recombinant IDPs requires extra care and caution, such as maintaining low temperature throughout the purification, the use of protease inhibitor cocktails and fast workflow. Even so, in th

SUBMITTER: Meszaros A 

PROVIDER: S-EPMC9687501 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature