Download Gilad Haran - Laboratoire Léon Brillouin

RÉPUBLIQUE FRANÇAISE
CENTRE NATIONAL DE LA RECHERCHE SCIENTIFIQUE - COMMISSARIAT A L'ÉNERGIE ATOMIQUE
LABORATOIRE LÉON BRILLOUIN
 33 (0) 1.69.08.52.41
Séminaire Physico-chimie & Biologie
Vendredi, 16 Juin 2006
11:00
Bât. 563 - salle 15
Gilad Haran
Chemical Physics Department, Weizmann Institute of Science, Rehovot 76100, Israel, e-mail:
[email protected]
Single-molecule protein folding
Fluorescence spectroscopy on the single-molecule level can provide a unique view of the
heterogeneous dynamics of folding proteins. We are using a custom-developed set of
methodologies, based on intra-molecular fluorescence resonance energy transfer (FRET), to
study folding in real time. In particular, surface-tethered lipid vesicles are used for mild
immobilization of protein molecules. This technique allowed us to obtain for the first time
folding and unfolding trajectories of individual molecules. In addition, experiments on freelydiffusing proteins open a window on the properties of their denatured states and show that they
undergo a globule-coil transition similar to that of homopolymers.
Laboratoire Léon Brillouin - CEA/Saclay - F - 91191 GIF-SUR-YVETTE
Télécopieur 33 (0) 1.69.08.82.61