ABSTRACT
The authors compared the spectral response of Zn-substituted horseradish peroxidase in a glycerol/water solvent to hydrostatic pressure at 2 K and ambient temperature. The low temperature experiments clearly demonstrate the presence of at least three different conformations with drastically different elastic properties. However, the main conformation, which determines the fluorescence spectrum at ambient temperature, did not show any significant difference between low and high temperature and pressure. The authors conclude that the local compressibility of the heme pocket of the protein depends only very weakly on temperature.
Subject(s)
Horseradish Peroxidase/chemistry , Temperature , Zinc/chemistry , Heme/chemistry , Hydrostatic Pressure , Protein Structure, Tertiary , Spectrometry, FluorescenceABSTRACT
We present quasielastic light scattering and dielectric spectra of the glass former alpha-picoline. At high temperatures the evolution of the susceptibility minimum is well described by the mode coupling theory (MCT). Below the critical temperature T(c) the simple scaling laws of MCT fail due to the appearance of the excess wing of the alpha process, which shows a universal evolution as a function of log(10)tau(alpha). Taking this into account, however, we observe the predicted cusplike anomaly of the nonergodicity parameter as well as a crossover to "white noise."
ABSTRACT
Precise low-frequency light scattering experiments on silica glass are presented, covering a broad temperature and frequency range ( 9 GHz
