Abstract
Pump-probe experiments in the infrared measure vibrational relaxation rates. Myoglobin, which is almost entirely helix in secondary structure, has an unusually long, nonexponential excited state relaxation generated by optically pumping at the blue side ( ) of the amide I band. The amino acid alanine and the predominantly sheet protein photoactive yellow protein do not have such a long-lived state, suggesting that the helix in proteins can support nonlinear states of 15 ps characteristic times.
- Received 11 October 1999
DOI:https://doi.org/10.1103/PhysRevLett.84.5435
©2000 American Physical Society