Journal
CHIRALITY
Volume 18, Issue 4, Pages 273-278Publisher
WILEY
DOI: 10.1002/chir.20254
Keywords
time-resolved circular dichroism; myoglobin
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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.
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