Final Activity Report Summary - PROSA (European Network on selection and analysis of protein-protein Interactions)
Protein-protein interactions are key mediators of functions of life in the cell. They play crucial roles in regulation of enzyme action, in signal transduction and inter-cellular communication. The network developed new methodologies and approaches in which protein-protein interactions were studied, predicted, analysed or experimentally altered, probed or evolved.
The SNAP-tag, commercialised by partner COVALYS and invented by partner EPFL was introduced as a new strategy for detecting protein-protein interactions in mammalian cell lysates based on the specific covalent cross-linking of two interacting partners.
Computational analysis of proteins as network graphs provided a novel way for deriving functional predictions from structure and sequence data.
Water-in-oil emulsion microdroplets were used to miniaturise biological assays to the pico-litre scale.
Protein-protein interactions validated split-ubiquitin data were used to define cytokinesis events in the bud neck region of the S. cervisiae cells.
In vitro evolutionary analysis gave insight on binding interaction involving protein-protein interfaces that share the evolvability features of enzymes, that is, the exploitation of promiscuous interactions and alternative binding configurations via generalist intermediates, and highlight the key role of compensatory stabilising mutations in facilitating the divergence of new functions.
The SNAP-tag, commercialised by partner COVALYS and invented by partner EPFL was introduced as a new strategy for detecting protein-protein interactions in mammalian cell lysates based on the specific covalent cross-linking of two interacting partners.
Computational analysis of proteins as network graphs provided a novel way for deriving functional predictions from structure and sequence data.
Water-in-oil emulsion microdroplets were used to miniaturise biological assays to the pico-litre scale.
Protein-protein interactions validated split-ubiquitin data were used to define cytokinesis events in the bud neck region of the S. cervisiae cells.
In vitro evolutionary analysis gave insight on binding interaction involving protein-protein interfaces that share the evolvability features of enzymes, that is, the exploitation of promiscuous interactions and alternative binding configurations via generalist intermediates, and highlight the key role of compensatory stabilising mutations in facilitating the divergence of new functions.