Carnegie Mellon University research enables location proteomics
For the first time, researchers have automatically grouped fluorescently tagged proteins from high-resolution images of cells. This technical feat opens a new way to identify disease proteins and drug targets by helping to show which proteins cluster together inside a cell.
The approach, developed by Carnegie Mellon University, outperforms existing visual methods to localize proteins inside cells, says Professor Robert F. Murphy, whose report, "Data Mining in Genomics and Proteomics," appears in an upcoming special issue of the Journal of Biomedicine and Biotechnology. "Our approach really enables the new field of location proteomics, which describes and relates the location of proteins within cells," said Murphy, a professor of biological sciences, machine learning, and biomedical engineering. "This work should provide a more thorough understanding of cellular processes that underlie disease."
Lauren Ward | EurekAlert!
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Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell.
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