Vibrational Echo Studies of Heme-Protein Dynamics

M. D. Fayer, Dana D. Dlott

Research output: Contribution to journalArticlepeer-review

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 languageEnglish (US)
Pages (from-to)324-337
Number of pages14
JournalACS Symposium Series
Volume676
StatePublished - Dec 1 1997

ASJC Scopus subject areas

  • Chemistry(all)
  • Chemical Engineering(all)

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