Kristian Schweimer

This study shows that RNA recognition by the Sxl protein depends on a dynamic conformational ensemble rather than a single structure, and perturbing this balance impairs RNA binding.

The paper investigates the energy landscape of coupled folding and binding in intrinsically disordered proteins, finding that electrostatic interactions compensate for energetic frustration.

The paper develops a deep mutational scanning framework to map variants to molecular functions in RBM20, identifying functional hotspots and therapeutic strategies for dilated cardiomyopathy.

This paper redesigns dsRBD domains to inhibit DHX9 helicase activity by targeting its autoregulatory interface, offering a computationally efficient strategy for therapeutic development.

AlphaDesign uses AlphaFold to design novel protein structures, including monomers, dimers, and higher-order complexes, showing structural integrity and conformational switching capabilities.

This paper identifies the RNA binding specificity of Hrp48, showing it binds the msl-2 mRNA 3' UTR independently of Sxl and Unr downstream of their binding sites.