Davide Mercadante

This paper introduces Martini3-NMR, a framework that integrates NMR data into coarse-grained simulations to improve the accuracy of protein conformational ensembles.

This study introduces NapshiftC, a neural network that uses NMR chemical shifts to improve coarse-grained simulations of intrinsically disordered proteins by incorporating secondary structure.

This study identifies redox-controlled dimerisation as a regulatory mechanism for ethylene biosynthesis enzyme ACO, revealing its role as a redox sensor in plant cells.

The paper investigates the ester bond crosslinking mechanism in bacterial adhesin proteins, confirming a protease-like mechanism through structural, functional, and computational analyses.

This study investigates the dynamic self-association of eIF4B's intrinsically disordered region using experiments and simulations, revealing its role in forming oligomers and phase separation.