Abstract
Broadband absorption measurements at millimeter-wave frequencies (40 GHz-170 GHz) are reported for several biological materials (lyophylized haemoglobin, lysozyme, silk keratin, poly-L-alanine). The measurements were extended over the temperature range from 4.2 K to 300 K using the novel oversized-cavity-technique (OCT). The millimeter-wave absorption of the dried materials was found to increase nearly exponentially with temperature and approximately as ν1·5 with frequency. This frequency and temperature dependence is quantitatively described as being due to three distinct relaxation processes on a picosecond time scale occuring in asymmetric double well potentials. These processes are most probably assigned to the NH⋯OC hydrogen bonds of the peptide backbone. For lysozyme the influence of hydration was investigated. The contribution of adsorbed water can be distinguished from the intrinsic proccesses by its different frequency dependence.
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© 1984 Plenum Press, New York
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Kremer, F., Poglitsch, A., Genzel, L. (1984). Picosecond Relaxations in Proteins and Biopolymers Observed By MM-Wave Spectroscopy. In: Adey, W.R., Lawrence, A.F. (eds) Nonlinear Electrodynamics in Biological Systems. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-2789-9_13
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DOI: https://doi.org/10.1007/978-1-4613-2789-9_13
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