Self-trapped states in proteins?

Robert H. Austin, Aihua Xie, Lex Van Der Meer, Michelle Shinn, George Neil

Research output: Contribution to journalArticlepeer-review

21 Scopus citations

Abstract

We show here that the temperature dependence of the amide I band of myoglobin shows evidence for a low-lying self-trapped state at 6.15 μm. We have conducted a careful set of picosecond pump-probe experiments providing results as a function of temperature and wavelength and show that this low-lying state has a 30 ps lifetime at 50 K, much longer than the relaxation time of the main amide I band at 50 K. Fits of the temperature dependence of thermal occupation of this state yield the result that it lies 280 K below the main amide I band. Since the gap energy of this state is approximately equal to room temperature, this self-trapped state can act as a transient store of vibrational energy at physiological temperatures in biomolecules and can help to direct the path of energy flow in a biomolecule under biological conditions.

Original languageEnglish (US)
Pages (from-to)S1693-S1698
JournalJournal of Physics Condensed Matter
Volume15
Issue number18
DOIs
StatePublished - May 14 2003

All Science Journal Classification (ASJC) codes

  • Materials Science(all)
  • Condensed Matter Physics

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