BMBF - HBPP - NGFN

Biomolecular Interaction Analysis (BIA) quantifies binding events between proteins (e.g. receptors, enzymes, antibodies), peptides, nucleotides, carbohydrates and small molecules, thus supporting functional genomic approaches. Based on findings provided by genomic analyses, BIA assigns functions to arbitrary listings of gene products within one proteome.
In the subproject, “Functional analysis of protein networks”, we try to identify, kinetically characterize and functionally describe proteins in interaction networks within the brain proteome. To this end, established and novel BIA-methods as well as classical methods in biochemistry, molecular biology and cellular biology are used.
Based on the analysis of selected protein networks, a more complete understanding of brain function will be generated and will be implemented into a bioinformatics platform. A focus is the functional characterization of protein-protein interactions in diseased tissues and cells. The relevance of cofactors and posttranslational modifications for protein function is analyzed. Phosphorylation patterns and the kinases involved herein are investigated employing Biacore technology and mass spectrometry. Model proteins, e.g. cAMP-dependent protein kinase and tau-protein are used as model systems for kinases and phosphorylation patterns, respectively.
In close collaboration with partners within the NGFN2 SMP Proteomics and KGs, interaction analysis is performed on an advanced level using state of the art BIA-equipment (Biacore instruments, AlphaScreen, BRET, FRET). Bioinformatics and toponomics will be used to identify relevant interaction partners which are validated in further analyses in vitro and in vivo.

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