Unified Simulation Platform for Interference Microscopy.

Interferometric scattering microscopy is a powerful technique that enables various applications, such as mass photometry and particle tracking. Here, we present a numerical toolbox to simulate images obtained in interferometric scattering, coherent bright-field, and dark-field microscopies. The scattered fields are calculated using a boundary element method, facilitating the simulation of arbitrary sample geometries and substrate layer structures.

Hyperphosphorylation of Human Osteopontin and Its Impact on Structural Dynamics and Molecular Recognition.

Protein phosphorylation is an abundant post-translational modification (PTM) and an essential modulator of protein functionality in living cells. Intrinsically disordered proteins (IDPs) are particular targets of PTM protein kinases due to their involvement in fundamental protein interaction networks. Despite their dynamic nature, IDPs are far from having random-coil conformations but exhibit significant structural heterogeneity.

Temperature as an Extra Dimension in Multidimensional Protein NMR Spectroscopy.

NMR spectroscopy is a particularly informative method for studying protein structures and dynamics in solution; however, it is also one of the most time-consuming. Modern approaches to biomolecular NMR spectroscopy are based on lengthy multidimensional experiments, the duration of which grows exponentially with the number of dimensions. The experimental time may even be several days in the case of 3D and 4D spectra.

The Ambivalent Role of Proline Residues in an Intrinsically Disordered Protein: From Disorder Promoters to Compaction Facilitators.

Intrinsically disordered proteins (IDPs) carry out many biological functions. They lack a stable three-dimensional structure, but rather adopt many different conformations in dynamic equilibrium. The interplay between local dynamics and global rearrangements is key for their function.