Magnetoresistance in two-dimensional array of Ge/Si was studied for a wide range of the conductance, where the transport regime changes from hopping to diffusive one. The behavior of magnetoresistance is similar for all samples; it is negative in weak fields and becomes positive with increasing of magnetic field. Negative magnetoresistance can be described in the frame of weak localization approach with suggestion that quantum interference contribution to the conductance is restricted not only by the phase breaking length but also by the localization length.

DEFECTS, MICROSTRUCTURES AND TEXTURES C451 and low (~10 9 cm -2 ) dislocation density has been characterized as cell walls and cell interiors respectively with compressive and tensile stresses in accordance with the quasi-composite model.The results are in gross agreement with earlier TEM studies.

The conditions of the deposition of the mixed cellulose acetovalerate ester Langmuir–Blodgett (LB) films are studied. The structure of films is examined by X-ray and electron diffraction methods, and atomic force microscopy. It was shown that LB films reveal the Y-type layer structure. A comparison between the macromolecule packing in LB films and macrofilms (bulk) was done. Modeling of the cellulose acetovalerate mono- and multilayer organization on the basis of the π–A isotherms and structural data was realized.

The process of multilayer assembly via layer-by-layer deposition of linear polyions and lysozyme have been studied. The films were fabricated on glass slides by alternate electrostatic adsorption of anionic poly(styrenesulfonate) (PSS), cationic poly(allylamine) (PAA) polyions and hen egg-white lysozyme. The multilayer build-up was monitored by the small-angle X-ray diffraction method. X-ray reflectivity curves from the films measured at different steps of the assembly reveal Kiessig fringes. From their periodicity the film thickness was calculated. The growth step for a PSS/PAA bilayer equals 37 Å. The thickness of the lysozyme layer equals 45 Å, which is close to dimensions of the lysozyme molecule determined by X-ray crystallography. An analysis of surface charges of the lysozyme molecule shows some preferentially positive charged regions, which are the most probable sites of interactions with negatively charged PSS.