Picosecond relaxations in hydrated lysozyme observed by mm-wave spectroscopy.
Dielectric absorption measurements at mm-wave frequencies (50 GHz. . . 150 GHz) are reported for lysozyme at different hydration levels. The measurements were extended over the temperature range from liquid helium to room temperature using the untuned cavity technique. For dried lysozyme (water content less than or equal to 0.5%, w/w) a nearly linear increase with frequency and an exponential increase with temperature of the absorption coefficient is observed between 50 K and 300 K. This frequency and temperature dependence is described by relaxation processes in asymmetric double-well potentials with relaxation times in the picosecond range. Hydration yields a nearly frequency-independent contribution to the absorption, which arises only at temperatures above 120 K. The frequency independence indicates relaxation rates for the bound water that are small compared to mm-wave frequencies. Thereby the contribution of bound water can clearly be distinguished from the fast intrinsic processes. An assignment of these picosecond relaxations to the NH . . . OC hydrogen bond of the peptide backbone is suggested.
D009113:Muramidase; D011487:Protein Conformation; D013055:Spectrophotometry, Infrared; D013696:Temperature; D014867:Water
D014867:Water; D009113:Muramidase