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.
| Original language | English |
|---|---|
| Pages (from-to) | 273-278 |
| Number of pages | 6 |
| Journal | Chirality |
| Volume | 18 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published - 9 May 2006 |
Keywords
- Myoglobin
- Time-resolved circular dichroism