CONICET | Buscador de Institutos y Recursos Humanos

Repeat proteins are constitutes by a variable number ofcopies of a given structural element that is tandemlyrepeated along a longitudinal axis. They mainly functionas protein-protein interactors with binding interfaces thatare not conserved along members of the same family butspecific for each interacting pair. These proteins havebeen extensively used as scaffolds for protein design thatare usually centered on the maximization of the stabilityof the repeat arrays. Although overall stability isimportant for obtaining molecules with enhancedsolubility and expression, natural occurring repeat proteinshave unstable designs that are relevant fortheir binding properties. Here we discuss the state of theart for repeat protein designs and the ideas of allowingenergetic conflicts for introducing enhanced functionalityin the arrays.