Translating the 4-letter code of RNA into the 22-letter alphabet of proteins is a central feature
of cellular life. The fidelity with which mRNA is translated during protein synthesis is …

The aminoacyl‐tRNA synthetases are prominently known for their classic function in the first
step of protein synthesis, where they bear the responsibility of setting the genetic code. Each …

Metal ion cofactors afford proteins virtually unlimited catalytic potential, enable electron
transfer reactions and have a great impact on protein stability,. Consequently …

Mitochondrial cristae, infoldings of the mitochondrial inner membrane, undergo aberrant
changes in their architecture with age. However, the underlying molecular mechanisms and …

Editing domains of aminoacyl tRNA synthetases correct tRNA charging errors to maintain
translational fidelity. A mutation in the editing domain of alanyl tRNA synthetase (AlaRS) in …

Protein folding can begin co-translationally. Due to the difference in timescale between
folding and synthesis, co-translational folding is thought to occur at equilibrium for fast …

Hundreds of non-proteinogenic (np) amino acids (AA) are found in plants and can in
principle enter human protein synthesis through foods. While aminoacyl-tRNA synthetase …

Misincorporation of amino acids in proteins expressed in Escherichia coli has been well
documented but not in proteins expressed in mammalian cells under normal recombinant …

Bacterial ribosomes stall on polyproline stretches and require the elongation factor P (EF-P)
to relieve the arrest. Yet it remains unclear why evolution has favored the development of EF …

Aminoacyl-tRNA synthetases hydrolyze aminoacyl adenylates and aminoacyl-tRNAs formed
from near-cognate amino acids, thereby increasing translational fidelity. The contributions of …