See how ligand-induced conformational changes can sharpen compound prioritization

The compound that binds best isn't always the one that works. Compounds with similar affinity and kinetics often behave very differently downstream — because binding alone doesn't reveal how a molecule reshapes its target.

Join us for this live webinar unveiling Molecular Friction Sensing on heliX⁺, a newly published approach for detecting ligand-induced conformational changes in proteins with sub-Ångström resolution under near-physiological conditions. Binding-induced modulation of protein structure is central to how many small-molecule drugs work, yet most screening platforms rely on affinity-based readouts that don't report conformational change. By resolving structural effects independently of affinity or kinetics, Molecular Friction Sensing adds an orthogonal decision-making dimension to hit-to-lead and lead optimization, helping you prioritize the most promising candidates earlier.

Presenting the science behind the recently released preprint, this session shows how the assay works, what it reveals, and how it fits alongside your existing biophysical toolkit.

What you'll learn

• How Molecular Friction Sensing detects ligand-induced conformational changes at sub-Ångström sensitivity
• Why a conformational readout adds information that affinity and kinetic data don't capture
• How to tell apart binders with similar affinities by their effect on protein structure
• Where the assay fits between routine binding assays and classical structural biology
• Results from the preprint, including the characterization of 22 confirmed carbonic anhydrase binders

Speaker: Prof. Dr. Ulrich Rant (Dresden University of Technology, Kurt Schwabe Institute for Sensor Technologies, Bruker Dynamic Biosensors, Dresden, Germany)