Sort   by:  
 Page size 
Proline-rich antimicrobial peptide apidaecin (Api) inhibits bacterial protein synthesis in a distinctive way. In vitro biochemical and structural studies showed that Api binds in the nascent peptide exit tunnel of the ribosome that has completed translation of the gene and has released the newly-syn...
ORGANISM(S): Escherichia coli 
2020-10-05 | PXD019012 | Pride
Sequence diversity of apidaecin-like peptides arresting the terminating ribosome
Proline-rich antimicrobial peptides (PrAMPs) inhibit bacterial ribosomes by binding to the polypeptide exit tunnel (PET) near the peptidyl transferase center. Api137, an optimized derivative of honeybee apidaecin, traps the release factor (RF) at the ribosome, thereby arresting the ribosomes at stop...
ORGANISM(S): Escherichia Coli 
Genome-wide effects of the antimicrobial peptide apidaecin on translation termination
Sort   by:  
 Page size