Ruben L. Gonzalez

This paper extends conventional TIRF microscopy to image single molecules in micromolar analyte backgrounds, enabling studies of weak biomolecular interactions.

This study uses single-molecule fluorescence microscopy to show that ATP binding enables eIF4F redistribution on mRNA, while ATP hydrolysis is required for eIF4F recycling during PIC loading.

This study shows an ultra-stable RNA stem-loop samples multiple conformations and adapts its flexibility to fold efficiently and resist unfolding.

This study uses smFRET to analyze the conformational changes of RF2 on the ribosome, revealing structural rearrangements essential for polypeptide release and potential antibiotic targets.

This study uses single-molecule fluorescence imaging to investigate how eIF4F recognizes and activates mRNA caps, revealing allosteric communication and subunit functions in the process.

This study reconstitutes a biochemically active yeast eIF3 complex and shows that eIF3a provides core RNA-binding activity, modulated by interactions with other subunits.

The paper introduces the RAD method to quantitatively describe subunit rotations in ribosomes and applies it to analyze ribosome structures across organisms.

This study uses time-resolved cryo-EM to visualize the conformational changes during bacterial 70S initiation complex formation and maturation into an elongation-competent complex.