Zeev Smilansky

TL;DR: Single-molecule fluorescence resonance energy transfer (smFRET) is employed to study structural dynamics over the first two elongation cycles of protein synthesis, using ribosomes containing either Cy3-labeled ribosomal protein L11 and A- or P-site Cy5- labeled tRNAs.

TL;DR: The results suggest that the distribution of pretranslocation tRNA states and posttranslocation pathways are correlated within each elongation cycle via communication between distant subdomains in the ribosome, but that this correlation between lengthening cycle intermediates does not persist into succeeding cycles.

TL;DR: It is demonstrated that FtTM allows quantitative comparison ofprotein synthesis between different cell types, monitoring effects of antibiotics and stress agents, and characterization of changes in spatial compartmentalization of protein synthesis upon viral infection.

TL;DR: Metal-enhanced fluorescence increased total photon emission of Cy3- and Cy5-labeled ribosomal initiation complexes near 50 nm silver particles 4- and 5.5-fold, respectively.

TL;DR: This work internalized tRNA labeled with organic fluorophores into live bacteria, applied single-molecule fluorescence imaging with single-particle tracking and localized and tracked single tRNA molecules over seconds, providing the first direct report on tRNA diffusion localization in live bacteria.