Artículo
A unifying motif of intermolecular cooperativity in protein associations
Accordino, Sebastian Roberto
; Rodriguez Fris, Jorge Ariel
; Appignanesi, Gustavo Adrian
; Fernández, A.
Fecha de publicación:
03/2012
Editorial:
Springer
Revista:
European Physical Journal E
ISSN:
1292-8941
e-ISSN:
1292-895X
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
At the molecular level, most biological processes entail protein associations which in turn rely on a 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.
Palabras clave:
PROTEINS
,
BINDING
,
HOT SPOTS
,
ALANINE SCANNING
Archivos asociados
Licencia
Identificadores
Colecciones
Articulos(IAM)
Articulos de INST.ARG.DE MATEMATICAS "ALBERTO CALDERON"
Articulos de INST.ARG.DE MATEMATICAS "ALBERTO CALDERON"
Articulos(INQUISUR)
Articulos de INST.DE QUIMICA DEL SUR
Articulos de INST.DE QUIMICA DEL SUR
Citación
Accordino, Sebastian Roberto; Rodriguez Fris, Jorge Ariel; Appignanesi, Gustavo Adrian; Fernández, A.; A unifying motif of intermolecular cooperativity in protein associations; Springer; European Physical Journal E; 35; 7; 3-2012; 1-7
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