| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 9577422 | Chemical Physics Letters | 2005 | 4 Pages |
Abstract
A time-resolved circular dichroism (CD) experiment is carried out on carbonmonoxy-myoglobin. The CD is measured with a sub-picosecond time resolution after ligand dissociation and the data are interpreted thanks to a classical CD calculation based on the polarizability theory. We observe a decrease of the CD signal in a few picoseconds and a sub-100Â ps relaxation towards steady-state deoxy-myoglobin values which we assign to a stress of the proximal histidine which relaxes with the global reorganization of the protein from its liganded geometry to its deliganded one.
Related Topics
Physical Sciences and Engineering
Chemistry
Physical and Theoretical Chemistry
Authors
Thibault Dartigalongue, François Hache,