Ekaterina Poliukhina, "Direct measurement of protein-protein interaction potentials by cryo-electron tomography"
A/1-106 - Seminarska soba fizike (F5)
Jamova
Protein-protein interactions control how proteins behave in solution, dictating aggregation, crystallization, phase separation, and the colloidal stability of formulations central to pharmacology, food science, and biotechnology. Predicting this behavior has long been difficult: theories borrowed from classical colloid science fail for proteins, which are irregularly shaped and chemically heterogeneous, and no direct experimental route to the underlying interaction potential has been available. Cryo-electron tomography now provides such a route. By reconstructing three-dimensional tomograms containing thousands of individual proteins, the spatial distribution of every particle can be recovered and converted, without any assumed functional form, into a measured interaction potential. Validated against analytical ultracentrifugation and small-angle X-ray scattering, the approach spans globular proteins from lysozyme to apoferritin and reveals how ionic strength, pH, temperature, and additives reshape their interactions.
Theoretical Biophysics and Soft Matter Group