Phys. Rev. Lett. 84, 5435–5438 (2000)Long-Lived Amide I Vibrational Modes in MyoglobinReceived 11 October 1999; published in the issue dated 5 June 2000 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 α helix in proteins can support nonlinear states of 15 ps characteristic times. © 2000 The American Physical Society URL:
http://link.aps.org/doi/10.1103/PhysRevLett.84.5435
DOI:
10.1103/PhysRevLett.84.5435
PACS:
87.15.-v, 36.20.-r
|
|
About | Terms and Conditions | Subscriptions | Search | Help
Use of the American Physical Society websites and journals implies that the user has read and agrees to our Terms and Conditions and any applicable Subscription Agreement. Physical Review®, Physical Review Letters®, Reviews of Modern Physics®, and Physical Review Special Topics® are trademarks of the American Physical Society.