Single molecule fluorescence spectroscopy and protein folding

Th, 05.07.2012 18:30  –   Th, 05.07.2012 19:30
Dr. William A. Eaton, Laboratory of Chemical Physics, NIDDK, National Institutes of Health, Bethesda, Maryland, USA
Magnus-Haus Berlin
Am Kupfergraben 7, 10117 Berlin, Germany

Event partner:
Wilhelm und Else Heraeus-Stiftung
Contact person:
Andreas Böttcher,
DPG Association:
Physikalische Gesellschaft zu Berlin e. V., Regionalverband Berlin/Brandenburg der Deutschen Physikalischen Gesellschaft e. V. (PGzB)  


Moderation: Prof. Dr. Roland Netz, Freie Universität Berlin

Berliner Physikalisches Kolloquium
im Magnus-Haus, Am Kupfergraben 7, 10117 Berlin
Eine gemeinsame Veranstaltung der Physikalischen Gesellschaft zu Berlin e.V. (PGzB),
der Freien Universität Berlin (FUB), der Humboldt-Universität zu Berlin (HUB),
der Technischen Universität Berlin (TUB) und der Universität Potsdam (UP),
gefördert durch die Wilhelm und Else Heraeus-Stiftung.

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.