Single molecule fluorescence spectroscopy and protein folding
Zeit
Sprecher:innen
- Dr. William A. Eaton
Dateien
Im Berliner Physikalischen Kolloquium im Magnus-Haus hat
Dr. William A. Eaton,
Laboratory of Chemical Physics, NIDDK, National Institutes of Health, Bethesda, Maryland, USA,
vorgetragen.
Zusammenfassung
One of the grand challenges in biophysical science is to understand how a disordered polypeptide chain folds into the unique three-dimensional structure that performs a biological function — the so-called protein folding problem. Progress in this area, as well as in the study of many other complex biomolecular processes, has come from the application of single molecule fluorescence spectroscopy. I will describe how Förster resonance energy transfer and a photon-by-photon analysis of single molecule fluorescence trajectories can be used to gain a deeper understanding of how proteins fold.