Four-photon Rayleigh-wing spectroscopy of α-chymotrypsin protein in water

Authors

  • A. F. Bunkin,

    Corresponding author
    1. Wave Research Center, Prokhorov General Physics Institute, Russian Academy of Sciences, 38 Vavilov Street, Moscow, 119991, Russia
    • Wave Research Center, Prokhorov General Physics Institute, Russian Academy of Sciences, 38 Vavilov Street, Moscow, 119991, Russia.
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  • A. U. Chikishev,

    1. Wave Research Center, Prokhorov General Physics Institute, Russian Academy of Sciences, 38 Vavilov Street, Moscow, 119991, Russia
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  • A. P. Gorchakov,

    1. Wave Research Center, Prokhorov General Physics Institute, Russian Academy of Sciences, 38 Vavilov Street, Moscow, 119991, Russia
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  • A. A. Nurmatov,

    1. Wave Research Center, Prokhorov General Physics Institute, Russian Academy of Sciences, 38 Vavilov Street, Moscow, 119991, Russia
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  • S. M. Pershin

    1. Wave Research Center, Prokhorov General Physics Institute, Russian Academy of Sciences, 38 Vavilov Street, Moscow, 119991, Russia
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Abstract

The low-wavenumber spectra of CCl4, Milli-Q water and aqueous solution of α-chymotrypsin protein were measured using four-photon coherent spectroscopy in the subterahertz range. Good coincidence of narrow peak positions in the four-photon spectra of liquid CCl4 with the rotational frequencies in the gas phase was observed for the first time. A new sharp (width ∼0.6 cm−1) resonance at ∼3 cm−1 was observed in the aqueous protein solution, in contrast with water. This difference was interpreted as an exhibition of low-wavenumber vibrations of large fragments of the protein molecule. Copyright © 2006 John Wiley & Sons, Ltd.

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