Stefan Duhr

TL;DR: The affinity of the small-molecule inhibitor quercetin to its kinase PKA was determined in buffer and human serum, revealing a 400-fold reduced affinity in serum, which may allow to make more reliable conclusions on protein functionality, and may facilitate more efficient drug development.

TL;DR: Using an all-optical microfluidic fluorescence method, results are presented that determine the effective charge of DNA and beads over a size range that is not accessible with electrophoresis, and support a unifying theory based on solvation entropy.

TL;DR: This review focuses on the theoretical background of MST and gives a detailed overview on various applications to demonstrate the broad applicability.

TL;DR: Flexibility in assay design qualifies MST for analysis of biomolecular interactions in complex experimental settings, which is demonstrated by addressing typically challenging types of binding events from various fields of life science.

TL;DR: This review presents recent progress and developments in MST technology and introduces alternative MST applications – such as determination of binding stoichiometries and binding modes, analysis of protein unfolding, thermodynamics and enzyme kinetics, as well as demonstrating the capability of MST to quantify high-affinity interactions with dissociation constants in the low picomolar (pM) range.