The ribosome is a large multifunctional complex composed of both RNA and proteins.
Biophysical methods are yielding low-resolution structures of the overall architecture of …

This review presents a description of the numerous eukaryotic protein synthesis factors and
their apparent sequential utilization in the processes of initiation, elongation, and …

Using single-molecule fluorescence spectroscopy, time-resolved conformational changes
between fluorescently labeled tRNA have been characterized within surface-immobilized …

Structures of 70 S ribosome complexes containing messenger RNA and transfer RNA
(tRNA), or tRNA analogs, have been solved by x-ray crystallography at up to 7.8 angstrom …

By using single-molecule fluorescence resonance energy transfer (smFRET), we observe
the real-time dynamic coupling between the ribosome, labeled at the L1 stalk, and transfer …

There is mounting evidence indicating that protein synthesis is driven and regulated by
mechanisms that direct stochastic, large-scale conformational fluctuations of the …

Crystal structures of tRNA mimics complexed with the large ribosomal subunit of
Deinococcus radiodurans indicate that remote interactions determine the precise orientation …

Protein synthesis is believed to be a dynamic process, involving structural rearrangements
of the ribosome. Cryo-EM reconstructions of certain elongation factor G (EF-G)-containing …

Determining the mechanism by which tRNAs rapidly and precisely transit through the
ribosomal A, P, and E sites during translation remains a major goal in the study of protein …

Ribosomal binding sites were investigated for the diverse group of antibiotics: anisomycin,
anthelmycin, blasticidin S, bruceantin, carbomycin, chloramphenicol, griseoviridin …