Paper Citing NAMD - Abstract
Espinoza-Fonseca, L. Michel
Aromatic residues link binding and function of intrinsically disordered proteins
MOLECULAR BIOSYSTEMS, 8:237-246, 2012
We have searched for intermolecular aromatic pairs in 77 protein-protein complexes of intrinsically disordered proteins (IDPs) to understand the role of pi-pi interactions in protein-protein interactions involving IDPs. We found that 40% of the complexes possess at least one intermolecular pair of aromatic residues. Analysis of composition, characteristics, location and the contribution to the free energy of binding showed that pi-pi interactions substantially contribute to binding by working as anchor residues, conformational locks, and ready-made recognition motifs required for specific binding. By using available experimental data we show that pi-pi interactions play a variety of roles that link binding of IDPs and their function in the cell. The results presented in this study pave the way to understand in atomic detail the inner workings of IDPs interaction networks.
