Résumé
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.
| langue originale | Anglais |
|---|---|
| Pages (de - à) | 273-278 |
| Nombre de pages | 6 |
| journal | Chirality |
| Volume | 18 |
| Numéro de publication | 4 |
| Les DOIs | |
| état | Publié - 9 mai 2006 |
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