Vibrational echo studies of protein dynamics

C. W. Rella, Alfred Kwok, Kirk Rector, Jeffrey R. Hill, H. A. Schwettman, Dana D. Dlott, M. D. Fayer

Research output: Contribution to journalArticlepeer-review


The first picosecond infrared vibrational echo experiments on a protein, myoglobin-CO, are described. The experiments were performed at temperatures ranging from 60 to 300 K with a midinfrared free electron laser tuned to 1945 cm-1. Below ∼185 K, the pure dephasing, T2*, displays a power law temperature dependence, T1.3. This behavior is reminiscent of that associated with the properties of low temperature glasses (<5 K) but is observed here at much higher temperatures. Above the solvent glass transition temperature, T2* is exponentially activated.

Original languageEnglish (US)
Pages (from-to)1648-1651
Number of pages4
JournalPhysical review letters
Issue number8
StatePublished - 1996

ASJC Scopus subject areas

  • Physics and Astronomy(all)


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