Heat treatment of thioredoxin fusions increases the purity of α-helical transmembrane protein constructs.

ABSTRACT: Membrane proteins play key roles in cellular signaling and transport, represent the majority of drug targets, and are implicated in many diseases. Their relevance renders them important subjects for structural, biophysical, and functional investigations. However, obtaining membrane proteins in high purities is often challenging with conventional purification steps alone. To address this issue, we present here an approach to increase the purity of α-helical transmembrane proteins. Our approach exploits the Thioredoxin (Trx) tag system, which is able to confer some of its favorable properties, such as high solubility and thermostability, to its fusion partners. Using Trx fusions of transmembrane helical hairpin constructs derived from the human cystic fibrosis transmembrane conductance regul

SUBMITTER: Schenkel M 

PROVIDER: S-EPMC8376418 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature