1 results match your criteria: "National Institutes of Health Frederick MD 21702 USA kylie.walters@nih.gov.[Affiliation]"
High-throughput assay exploiting disorder-to-order conformational switches: application to the proteasomal Rpn10:E6AP complex.
Chem Sci
March 2024
Protein Processing Section, Center for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health Frederick MD 21702 USA
Article Synopsis
- Conformational switching in proteins, especially those with intrinsically disordered regions, is influenced by protein interactions, which can be studied using a newly developed fluorescence-based assay.
- The assay focuses on the E3 ligase E6AP and its effect on the Rpn10 AZUL-binding domain (RAZUL), showing how E6AP induces a transition from disorder to order in RAZUL.
- Different fluorophores (acrylodan and Atto610) were tested for their spectral responses during this process, allowing for high-throughput screening of compounds that disrupt the Rpn10:E6AP interaction and demonstrating the assay's wide applicability to similar molecular transitions.