The first picosecond infrared vibrational echo experiments on a protein, myoglobin-CO, are described. The experiments, performed over a temperature range of 50-300K, with native and mutant myoglobin in different solvents, provide information about protein dynamics occurring on the 10-12-10-10 s time scales, which influence the vibrational transition of the CO ligand bound to the active site. The experiments reveal the existence of a protein energy landscape with a relatively flat distribution of energies between conformational minima, which interconvert via tunneling at lower temperature and by activated processes at ambient temperature.
|Original language||English (US)|
|Number of pages||14|
|Journal||ACS Symposium Series|
|State||Published - Dec 1 1997|
ASJC Scopus subject areas
- Chemical Engineering(all)