Two approaches that use femtosecond infrared pulses to examine protein dynamics by means of nonlinear IR spectroscopy are described. In the first we dissect the featureless peptide amide-I band and introduce two-dimensional IR spectra [1]. In the second, the correlation function of the frequency fluctuations of a vibrational mode in the active site of carbonic anhydrase and heme pocket of hemoglobin is determined by three-pulse IR photon echoes [2]. These experiments permit the study of ultrafast dynamics without the requirement of chromophores.
CITATION STYLE
Hochstrasser, R. M., Hamm, P., & Lim, M. (1998). Femtosecond dynamics, two dimensional infrared spectroscopy and echoes of protein vibrations. Springer Series in Chemical Physics, 63, 653–657. https://doi.org/10.1007/978-3-642-72289-9_198
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