Hydrogen bonds stabilize the crystal structures of most proteins. In the aqueous environment, they lie at the edge of stability and hence are easily formed and broken, especially those with high free energy. Using a Boltzmann-like formalism, empirical sampling of their geometry leads to free energy estimates, thus allowing a priori predictions of protein regions primed for structural rearrangement. One among diverse applications involves viral glycoproteins and capsids, namely those proteins employed by viruses to fuse with or penetrate the host cell. Here the methods are used to identify sites of interest for vaccine/drug/testing development, in particular for the SARS CoV-2 virus that causes COVID-19.
Please click the link below to register to the webinar: