Calculation of the circular dichroism spectra of carbon monoxy- and deoxy myoglobin: interpretation of a time-resolved circular dichroism experiment. - École polytechnique Access content directly
Journal Articles Journal of Chemical Physics Year : 2005

Calculation of the circular dichroism spectra of carbon monoxy- and deoxy myoglobin: interpretation of a time-resolved circular dichroism experiment.

Abstract

A calculation of the circular dichroism (CD) spectra of carbon monoxy- and deoxy myoglobin is carried out in relation with a time-resolved CD experiment. The calculation is based on the polarizability theory and the parameters are adjusted to fit the experimental absorption and CD spectra. By performing the calculation for intermediate configurations of the protein, we are able to propose an explanation of the CD structure observed on a sub-100 ps time scale. The role of the proximal histidine is, in particular, clearly demonstrated in the first step of the myoglobin relaxation from its liganded to it deliganded form.
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Dates and versions

hal-00827924 , version 1 (15-05-2014)

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Thibault Dartigalongue, François Hache. Calculation of the circular dichroism spectra of carbon monoxy- and deoxy myoglobin: interpretation of a time-resolved circular dichroism experiment.. Journal of Chemical Physics, 2005, 123 (18), pp.184901. ⟨10.1063/1.2041467⟩. ⟨hal-00827924⟩
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