Riccardo Pellarin

This study develops a kinetic model to describe cross-link formation in protein-protein interactions and identifies optimal cross-linker concentrations for maximizing cross-link yield.

The paper presents a computational method to predict PROTAC-compatible protein-protein interfaces using docking and scoring techniques, achieving high accuracy in benchmark tests.

The paper introduces a graph-based method to build atomic protein models from cryo-EM density maps using residue co-evolution data to improve segmentation and sequence assignment.

The paper introduces a Bayesian scoring function to rank structural models using cryo-EM data and other information, validated on known complexes and implemented in an open-source platform.

This paper introduces a method to simultaneously determine protein structure and dynamics from cryo-electron microscopy data, applied to the STRA6 receptor.