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En sus 88 años de historia, la misión de nuestro instituto ha sido realizar una  investigación de excelencia en fisicoquímica fundamental y aplicada, contribuyendo a la formación de varias generaciones de  científicos del máximo nivel. La visión de nuestro instituto es ser una referencia internacional en investigación multidisciplinar enfocada a resolver los retos actuales de nuestra sociedad en ámbitos de salud, biotecnología, nuevos materiales y medioambiente.



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Plausible approximations to the sequences of ancestral proteins can be derived from the sequences of their modern descendants. Proteins encoded by the ancestral reconstructed sequences can be prepared in the laboratory and subjected to experimental scrutiny.

 Besides their use over the last ~25 years as molecular tools to address important evolutionary issues, more recent work suggests the biotechnological potential of such “resurrected” ancestral proteins. Ancestral proteins certainly differ from their modern counterparts in terms of sequence. This is particularly the case when “old” phylogenetic nodes are targeted. Indeed, reconstructed sequences of Precambrian proteins often show large numbers of amino acid differences with their modern descendants. More relevant, however, is the fact that ancestral proteins were adapted to intra-cellular and extra-cellular environments that likely depart from environments that host modern proteins. As a result, resurrected ancestral proteins could be expected to display “unusual” properties to some extent. Experimental and computational work has specifically discussed high stability, substrate and catalytic promiscuity, conformational flexibility/diversity and altered patterns of interaction with other sub-cellular components.
I will summarize and discuss this recent work as well as very recent attempts to explore the biotechnological and, more specifically, protein-engineering applications of resurrected ancestral proteins.

SEMINAR’S DATE, TIME AND PLACE: Wednesday, 17 January 2018, 15:30. Assembly Hall.

SPEAKER: Juan Manuel Sánchez Ruiz