The angle dependencies of diffuse x-ray scattering intensities were studied in a wide range of angles from 3 to 80 degrees for water-soluble and membrane proteins with a different structural organization: alpha-helical protein myoglobin, alpha-helical protein serum albumen, alpha + beta protein lysozyme, and transmembrane proteins of photosynthetic reaction centers (RC) from purple bacteria Rhodobacter sphaeroides, and Blastochlorii (Rhodopseudomonas) viridis containing cytocrome c, situated out side the membrane, and for H and L+M subunits of membrane protein of reaction center from Rb. sphaeroides for various hydration degrees. The hydration/dehydration process was studied for water-soluble proteins (within hydration range from h = 0.05 to h = 1). The hydration/dehydration process appears to be reversible. All water-soluble proteins show a 10 angstroms peak, and proteins of reaction center do not show this peak. A quantitative comparable study of the behaviour for of the 10 angstroms peak different proteins the degree of lysozyme hydration increases from h = 0.05 to h = 0.45, the protein structure slightly changes (most probably the motifoffolding), the structure of myoglobin in solution is slightly different from the structure in crystal. By taking into account the changes in the shape and intensity of the 10 angstroms peak only, it is impossible to make the conclusion about structural changes in other proteins studied. A correlation between the structural changes observed and dynamic and functional properties of proteins is discussed.

A comparative study of the dynamics of protein secondary structure elements by the example of alpha-helices, of myoglobin, barnase, polylysine, and polyglycine and beta-layers of barnase and GFP was carried out by the methods of molecular dynamics. The effective Young's moduli of both free secondary structure elements and those built in the protein, globule were determined. A heterogeneity of the elastic properties, of the secondary structure elements Was found. The melting of myoglobin alpha-helix in a virtual viscous medium was studied.

Limited diffusion of the ferric hydroxide (ferrihydrite) nanoparticles in the polymeric network of the AG 50W-X2 sulfonated cation exchanger solvated with aqueous solutions of glycerol (70 and 90 wt.%) was studied in the temperature interval from 90 to 293 K. The Mössbauer spectra were obtained in three windows (250, 25, and 5 mm/s) because of large line broadenings observed in the experiment. The procedure of “seaming” of the time-dependent correlation functions <[Δx( t )] 2 > obtained by the Fourier transform analysis of the initial Mössbauer spectra made it possible to observe the behavior of the function in the extremely wide time range from 0.4 to 360 ns. The observed plateau of the function at long times is a direct proof of the limited nature of the motion. The experimental data were interpreted in the framework of physical models of limited diffusion.