Última modificación: 04/03/2020 - 12:12
De novo design of proteins for tailoring structures and binding functions
Traditional strategies to engineer proteins for biocatalysis, small-molecule biosensing or therapeutics, rely on finding existing proteins having already a similar function or, at least, a suitable geometry and enough stability to tolerate mutations to achieve the new function. This dependence on existing protein structures can be a limitation for certain applications and, instead, computationally designing proteins, de novo, with custom-made structures should be more effective. We have identified key principles for protein design and then developed a series of computational strategies in Rosetta to de novo design protein folds with curved beta-sheets for building ligand-binding cavities and beta-sandwiches for tailoring antibody frameworks. I will also discuss our design work on helical proteins to mimik interfaces and target nucleosomal DNA for chromatin research. The recent de novo protein revolution now allows to explore a vast sequence and structural space for tailoring a wide range of biotechnological solutions, and ultimately advance our understanding on how proteins fold and work.
LUGAR Y HORA: Sala de Conferencias, Edif. I+D, Campus Rio Ebro
FECHA Y HORA: VIERNES 13 de MARZO a las 12:30h