Ponente
Descripción
NMR spectroscopy is a valuable structural biology method to study proteins in solution in terms of molecular details, dynamics, and interaction with substrates and other biomacromolecules to be functional. We investigated the bacterial protein SlyD (sensitive to lysis protein D), which is a molecular chaperone and prolyl cis/trans isomerase (PPIase). After solving the three-dimensional structure by NMR, we could reveal the molecular mechanism of how SlyD functions, which is a dynamic coupling between the chaperone and PPIase domain. Knowledge of this mechanism was key for the development of the next generation Elecsys Anti-SARS-CoV-2 S test of Roche Diagnostics to quantify the antibody level in human blood after a COVID-19 infections or vaccination. This test employs the receptor binding domain of the corona virus as fusion protein with two SlyD molecules, which are essential as molecular chaperones to facilitate the antigen-antibody reaction.
