Colin D. Kinz-Thompson

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 identifies a pre-active intermediate in GPCR activation and shows how dimer interactions influence signaling efficacy and functional diversity.

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.

This paper introduces a new resolution metric for structural biology that quantifies how effectively biomolecular structural information is captured across different length scales.