Long-lived amide I vibrational modes in myoglobin

Aihua Xie, Lex van der Meer, Wouter Hoff, Robert H. Austin

Research output: Contribution to journalArticlepeer-review

197 Scopus citations


Pump-probe experiments in the infrared measure vibrational relaxation rates. Myoglobin, which is almost entirely α helix in secondary structure, has an unusually long, nonexponential excited state relaxation generated by optically pumping at the blue side (5.85μm) of the amide I band. The amino acid alanine and the predominantly β sheet protein photoactive yellow protein do not have such a long-lived state, suggesting that the a helix in proteins can support nonlinear states of 15 ps characteristic times.

Original languageEnglish (US)
Pages (from-to)5435-5438
Number of pages4
JournalPhysical review letters
Issue number23
StatePublished - 2000

All Science Journal Classification (ASJC) codes

  • General Physics and Astronomy


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