From duplication to fusion: Expanding Dayhoff's model of protein evolution.

Dayhoff's hypothesis suggests that complex proteins emerged from simpler peptides or domains, which duplicated and fused to create more complex proteins and novel functions. These processes expanded and diversified the protein repertoire within organisms. Extensive studies and reviews over the past two decades have highlighted the impact of gene duplication on protein evolution.

Single-Molecule Observation of Ligand Binding and Conformational Changes in FeuA.

The specific binding of ligands by proteins and the coupling of this process to conformational changes is fundamental to protein function. We designed a fluorescence-based single-molecule assay and data analysis procedure that allows the simultaneous real-time observation of ligand binding and conformational changes in FeuA. The substrate-binding protein FeuA binds the ligand ferri-bacillibactin and delivers it to the ATP-binding cassette importer FeuBC, which is involved in bacterial iron uptake.