Observation of ultrafast conformational changes in carboxy-myoglobin by time-resolved circular dichroism

Thibault Dartigalongue (1) , François Hache (1)

1 LOB - Laboratoire d'optique et biosciences

A time-resolved circular dichroism experiment is carried out on carboxy-myoglobin. CD is measured with a sub-picosecond time resolution after ligand dissociation. We observe a decrease of the CD signal in a few picoseconds followed by a 100 ps relaxation towards the deoxy-myoglobin values. Thanks to a calculation developed after the polarizability theory, we are able to assign this signal to a global reorganization of the protein conformation.

Thibault Dartigalongue, François Hache. Observation of ultrafast conformational changes in carboxy-myoglobin by time-resolved circular dichroism. Sixth International Topical Conference on Optical Probes of Conjugated Polymers and Biosystems, Apr 2005, India. pp.414-417, ⟨10.1016/j.synthmet.2005.09.026⟩. ⟨hal-00098229⟩