Abstract
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) |
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Pages (from-to) | 324-337 |
Number of pages | 14 |
Journal | ACS Symposium Series |
Volume | 676 |
State | Published - 1997 |
ASJC Scopus subject areas
- Chemistry(all)
- Chemical Engineering(all)