Structural Dynamics of Translation
We study the structural dynamics of macromolecules using ensemble and single molecule fluorescent methods. Our main experimental approaches are based on Förster resonance energy transfer (FRET), which has proven to be a powerful tool for studying the movements within macromolecules and macromolecular complexes. The kinetics of conformational changes in macromolecules is followed by FRET combined with stopped-flow fast-mixing experiments. We also measure FRET in single molecules using total internal reflection fluorescent (TIR) microscopy. Single-molecule measurement techniques have revolutionized molecular biology by providing previously unobtainable data that were masked in ensemble measurements because of signal averaging in the heterogeneous and non-synchronized population of the molecules.
Our research is predominately focused on the mechanism of protein synthesis. The ribosome is a central component of cell metabolism, an extremely complex and highly dynamic machine. We are interested to learn how the structural dynamics of the ribosome and ribosomal ligands enable protein synthesis. We also investigate the folding and dynamics of structured mRNA molecules, including mRNAs containing riboswitches or structural elements that induce programmed ribosomal frameshifting.
- Initiation factor 2 stabilizes the ribosome in a semirotated conformation.Proc Natl Acad Sci U S A. 112, 15874-9. (2015 Dec 29).
- Ribosome subunit joining frozen in time.Structure. 23, 977-8. (2015 Jun 02).
- Movement of elongation factor G between compact and extended conformations.J Mol Biol. 427, 454-67. (2015 Jan 30).