Harold D. Kim

TL;DR: Using single-molecule fluorescence spectroscopy, time-resolved conformational changes between fluorescently labeled tRNA have been characterized within surface-immobilized ribosomes proceeding through a complete cycle of translation elongation, suggesting that the growing peptide chain plays a role in modulating fluctuations between hybrid and classical states.

TL;DR: This work has developed a general method to label specifically the prokaryotic ribosome by hybridization of fluorescent oligonucleotides to mutated ribosomal RNA.

TL;DR: The state-of-the-art in single-molecule FRET (smFRET) has become a mainstream technique for studying biomolecular structural dynamics as mentioned in this paper, which has generated significant progress in sample preparation, measurement procedures, data analysis, algorithms and documentation.

TL;DR: It is suggested that formation of the first peptide bond destabilizes the SD interaction, resulting in the weakening of the force with which the ribosome grips an mRNA.

TL;DR: The relationship of loop lifetime to loop size revealed a critical transition in bending stress, and the result is in quantitative agreement with the kinkable worm-like chain model, and can reproduce previously reported looping probabilities of dsDNA over the range between 50 and 200 bp.