Vitalii I. Gol'danskii

Rayleigh Scattering of Mössbauer Radiation (RSMR) Data, Hydration Effects and Glass-like Dynamical Model of Biopolymers

Specific features of the Rayleigh Scattering of Mossbauer Radiation (RSMR) technique in the study of biological systems are described. Experimental data show that the temperature and hydration degree are the principal parameters which influence intramolecular mobility in biopolymers. Data in temperature dependencies of elastic fraction, f, and spectrum lineshape doesn’t fit either Debye or Einstein models of solids or the free diffusion in liquids and demand for their explanation a multimode approximation (i.e. a wide spectrum of correlation times, at T = 293K from 10-6 s to 10-12 – 10-13s). On the basis of RSMR, low temperature specific heat and x-ray dynamical analysis data and from the general considerations that macromolecule must be in a non-equilibrium state (an independent confirmation of this fact comes from the kinetic model of protein folding) a glass-like dynamical model of biopolymers is formulated. A possible interpretation of RSMR data shows that fluctuatively prepared tunneling between quasi-equilibrium positions (QEP) can prevail activated transitions up to a room temperature.

Dynamics of protein-water systems revealed by Rayleigh scattering of Mössbauer radiation (RSMR)

A critical review of recent studies of protein dynamics by the RSMR technique is given. The main approximations in quantitative analyses of RSMR data are discussed and conclusions about dynamical properties of protein and interprotein water, deduced from experiments, are described.

RSMR study of the hydration effect on the dynamics of some globular proteins

The dependence of the Mössbauer elastic scattering fraction on the hydration degree (h) has been studied for hydrated samples of human albumen (HSA), lysozyme and trypsin pancreatic inhibitor, within the range ofh between 0–0.75 g H2O/g protein at 295 K, and for HSA with different hydration degrees (0.03, 0.25, 0.41, 0.65) in the temperature range between 100–320 K. An increase of the hydration degree forh>0.1 atT>200 K has been shown to result in the release of intramolecular mobility in proteins.

The mobility of chromatophore membranes from Ectothiorhodospira Shaposhnikovii revealed by Rayleigh scattering of Mössbauer radiation (RSMR) experiments

AbstractChromatophores from Ectothiorhodospira Shaposhnikovii in solvents of different viscosity were investigated by RSMR experiments in the temperature range between 112 K and room temperature. Additional RSMR-experiments were done on solvents only. The mobility of the molecules and within the molecules is the given by the Debye-Waller factor which yields the meansquare displacement,

Some still open questions of relaxational COheme rebinding

\overline {\left\langle {x^2 } \right\rangle }

Temperature dependence of the dynamics of ultrafine particles in a polymeric network

, averaged over the atoms in the system. The mobility of the atoms of the chromatophores roughly follows the mobility of the atoms of the solvents. At low temperatures the mobility of the chromatophores remains slightly larger than the mobility of the frozen solvent. At room temperature, however,

Vitrification effects in water—protein systems

\overline {\left\langle {x^2 } \right\rangle }