I. P. Suzdalev

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, n

A METHOD OF MOSSBAUER FOURIER SPECTROSCOPY FOR DETERMINATION OF THE BIOPOLIMER COORDINATE CORRELATION FUNCTIONS

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Study of the Dynamics of Hydrated Proteins and Protein­ Bound Water by Rayleigh Scattering of Mossbauer Radiation (RSMR)

n, 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, n

Electronic state of the iron atom in heme and heme protein molecular motion studied by Mössbauer spectroscopy

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SIZE EFFECTS IN FINE PARTICLES OF Fe3O4

n of the chromatophores remains significantly smaller.Chromatophores in a glycerol-water mixture (0.001 M Tris-HCl buffer) and in water (0.05 M Tris-HCl buffer) show a different dynamic behaviour. A region with enhanced mobility near T=180 K was indicated for the chromatophores in the glycerolwater mixture.A correlation has been suggested between the rate of electron transfer from the primary to the secondary quinone and the increase of the conformational mobility of the chromatophores in glycerol-water mixture.