INSTITUTO ARGENTINO DE MATEMATICA ALBERTO CALDERON
Unidad Ejecutora - UE
"A unifying motif of intermolecular cooperativity in protein associations"
S. ACCORDINO; J. A. RODRÍGUEZ FRIS; G. A. APPIGNANESI; A. FERNÁNDEZ
1292-8941 - EUROPEAN PHYSICAL JOURNAL E
EDP Sciences, Società Italiana di Fisica and Springer-Verlag
Lugar: BERLIN; Año: 2012 vol. 35 p. 59 - 59
At the molecular level, most biological processes entail protein associations which in turn rely ona small fraction of interfacial residues called hot spots. Our theoretical analysis shows that hot spots share a unifying molecular attribute: they provide a third-body contribution to intermolecular cooperativity. Such motif, based on the wrapping of interfacial electrostatic interactions, is essential to maintain the integrity of the interface. Thus, our main result is to unravel the molecular nature of the protein association problem by revealing its underlying physics and thus by casting it in simple physical grounds. Such knowledge could then be exploited in rational drug design since the regions here indicated may serve as blueprints to engineer small molecules disruptive of protein-protein interfaces.