| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10618757 | Synthetic Metals | 2005 | 4 Pages |
Abstract
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 100Â 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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Physical Sciences and Engineering
Materials Science
Biomaterials
Authors
Thibault Dartigalongue, François Hache,