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

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.

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Additional Info

Field	Value
Source	Synthetic Metals
Author	Dartigalongue, Thibault, Hache, François
Maintainer	CCSD
Last Updated	May 5, 2026, 13:33 (UTC)
Created	May 5, 2026, 13:33 (UTC)
Identifier	hal-00098229
Language	en
contributor	Laboratoire d'optique et biosciences (LOB) ; École polytechnique (X) ; Institut Polytechnique de Paris (IP Paris)-Institut Polytechnique de Paris (IP Paris)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)
creator	Dartigalongue, Thibault
date	2005-04-01T00:00:00
harvest_object_id	a1c53d7a-1d0a-445e-856c-a21cee58c71c
harvest_source_id	3374d638-d20b-4672-ba96-a23232d55657
harvest_source_title	test moissonnage SELUNE
metadata_modified	2025-08-20T00:00:00
relation	info:eu-repo/semantics/altIdentifier/doi/10.1016/j.synthmet.2005.09.026
set_spec	type:COMM