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Protein-protein interactions play important roles in most cellular processes. Proteins interact through chemical and structural complementarity of their mutual binding sites. Amino acids found in physical proximity form non-covalent interactions that stabilize the complex. Here we studied the evolution of PPI interfaces applying directed in vitro evolution on a random TEM library expressed on yeast surface. Our study focused on two specific questions: 1) How plastic is a well-defined PPI interface? For that purpose the TEM library was softly selected against its high affinity binder BLIP and analyzed by deep sequencing. 2) Is it possible to evolve new PPIs? Here the monomeric TEM library was selected against TEM-WT and other proteins to create new binders. Our results show that PPI interfaces are plastic and easily formed, hence evolution must actively act to prevent promiscuous protein binding. One mechanism which seems to be applied by nature for that purpose is keeping wild type proteins below their potential stability in a way that they are easily destabilized upon mutation.

author of the book “scientific paper writing - a survival guide”

Motivated by the lack of signals of New Physics in indirect searches and by the fact that the SM posses various accidental and approximate symmetries, I will talk about extensions at the electroweak scale of the SM that automatically preserve such symmetries. I will finally comment about cosmological as well as phenomenological implications of such a framework.