Macrolide antibiotics inhibit protein synthesis by targeting the bacterial ribosome. They bind
at the nascent peptide exit tunnel and partially occlude it. Thus, macrolides have been …

Traditional annotation of protein-encoding genes relied on assumptions, such as one open
reading frame (ORF) encodes one protein and minimal lengths for translated proteins. With …

The quality of diffraction data obtained using silver and molybdenum microsources has been
compared for six model compounds with a wide range of absorption factors. The …

Macrolides represent a large family of protein synthesis inhibitors of great clinical interest
due to their applicability to human medicine. Macrolides are composed of a macrocyclic …

The ribosome is one of the main antibiotic targets in the bacterial cell. Crystal structures of
naturally produced antibiotics and their semi-synthetic derivatives bound to ribosomal …

The biogenesis, folding, and structure of α-helical membrane proteins (MPs) are important to
understand because they underlie virtually all physiological processes in cells including key …

Methicillin resistant Staphylococcus aureus strains pose a serious treatment problem
because of their multi-drug resistance (MDR). In staphylococcal strains, resistance to …

Small proteins, here defined as proteins of 50 amino acids or fewer in the absence of
processing, have traditionally been overlooked due to challenges in their annotation and …

Macrolides and ketolides comprise a family of clinically important antibiotics that inhibit
protein synthesis by binding within the exit tunnel of the bacterial ribosome. While these …

Macrolide resistance mechanisms can be target-based with a change in a 23S ribosomal
RNA (rRNA) residue or a mutation in ribosomal protein L4 or L22 affecting the ribosome's …