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A recent "Nature Structural and Molecular Biology" paper by the Beltrao group (IMSB) in collaboration with the  Elofsson group (Stockholm University, Sweden) have predicted complex structures for 65,000 pairs of human proteins and identify interfaces harbouring disease mutations.

A recent "Cell Reports" paper by the Sauer group (IMSB) quantified non-enzymatic acetylation in central metabolism by intact protein mass spectrometry, demonstrating a novel regulation of glycolytic flux through acetylphosphate-dependent acetylation.

Researchers have for the first time elucidated the structure of a very small enzyme located in cell membranes. In multicellular organisms, this enzyme uses a complex mechanism to attach sugar molecules to proteins, which are then directed to the cell surface and perform their function in cell-cell communication. The findings could accelerate the development of new protein-based drugs.

A recent "Nature Microbiology" paper by the Hardt group in collaboration with Piel, von Mering and Sourjik groups shows that chemotaxis towards interspecies quorum sensing signal autouinducer-2 promotes gut colonization and co-existence of E. coli strains in the murine gut.

A recent collaborative effort of the Tajkhorshid lab (University of Illinois) and Locher lab (ETHZ) has been published in "PNAS". The authors revealed differential binding dynamics of varied bound ligands in multidrug transporter ABCG2 and that phospholipids from the cellular membrane, but not cholesterol, can penetrate into the drug binding pocket of ABCG2.