Time-resolved circular dichroism in carbonmonoxy-myoglobin: The central role of the proximal histidine - École polytechnique Access content directly
Journal Articles Chirality Year : 2006

Time-resolved circular dichroism in carbonmonoxy-myoglobin: The central role of the proximal histidine

Abstract

A calculation of the circular dichroism (CD) spectra of carbonmonoxy-and deoxy-myoglobin is carried out in relation to a time-resolved CD experiment. This calculation allows us to assign a dominant role to the proximal histidine in the definition of the electronic normal modes and to interpret the transient CD structure observed in a strain of the proximal histidine. This strain builds up in 10 ps and relaxes in 50 ps as the protein evolves towards its deoxy form. Cop. 2006 Wiley-Liss, Inc.

Dates and versions

hal-00827922 , version 1 (31-05-2013)

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Thibault Dartigalongue, François Hache. Time-resolved circular dichroism in carbonmonoxy-myoglobin: The central role of the proximal histidine. Chirality, 2006, 18 (4), pp.273. ⟨10.1002/chir.20254⟩. ⟨hal-00827922⟩
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