Vibrational Echo Studies of Heme-Protein Dynamics

M. D. Fayer, Dana D. Dlott

Research output: Contribution to journalArticlepeer-review


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 languageEnglish (US)
Pages (from-to)324-337
Number of pages14
JournalACS Symposium Series
StatePublished - 1997

ASJC Scopus subject areas

  • Chemistry(all)
  • Chemical Engineering(all)


Dive into the research topics of 'Vibrational Echo Studies of Heme-Protein Dynamics'. Together they form a unique fingerprint.

Cite this