Publications by authors named "Odinokov S"

This paper describes the experiment on multiplexing recording using a phase mask to create augmented reality waveguides. The study is distinguished by the application of photo-thermo-refractive glass as both holographic and substrate materials. The presented approach allows us to obtain the diffraction efficiency above 15% in each of the multiplexed gratings for sevenfold recording.

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All of the existing holographic wavefront sensors are either bulky or have low accuracy of measuring wavefront aberrations. In this paper, we present an improvement of the holographic method of measuring wavefront aberrations using computer-generated Fourier holograms. The novelty of this work lies in the proposed approach to the synthesis of Fourier holograms, which are implemented using phase-only SLM.

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An augmented reality display based on a planar waveguide made in photo-thermo-refractive glass had been demonstrated. The monolithic integration of multiplexed volume Bragg gratings with the waveguide platform provided in/out-coupling and image transmission from a portable projector. Design and calculation of the grating configuration was performed.

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In interferential linear displacement sensors, accurate information about the position of the reading head is calculated out of a pair of quadrature (sine and cosine) signals. In double grating interference schemes, diffraction gratings combine the function of beam splitters and phase retardation devices. Specifically, the reference diffraction grating is located in the reading head and regulates the phase shifts in diffraction orders.

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The present article is dedicated to the problem of computer-generated holograms application for measurement of optical wavefront curvature with high precision. A holographic wavefront sensor scheme based on a phase-only spatial light modulator, which is used for CGH displaying, is proposed. The presented optical scheme and processing algorithm are validated with numerical simulations and experimental modelling.

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Utilization of computer generation of holographic structures significantly simplifies the optical scheme that is used to record the microholograms in a holographic memory record system. Also digital holographic synthesis allows to account the nonlinear errors of the record system to improve the microholograms quality. The multiplexed record of holograms is a widespread technique to increase the data record density.

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Holography is known to be a prospective tool for storing large amounts of digital information, providing long lasting safety and high speed data access. In this paper, we present a new approach to holographic memory system design. Our method is based on an application of discrete Fourier-transform calculations to encode two-dimensional binary data pages as computer-generated amplitude Fourier holograms (CGFHs).

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The effect of solution ionic strength, calcium ion concentration, and temperature on spatial structure of cyprein was examined by CD, UV, and fluorescence spectroscopy. The secondary structure of the cyprein molecule was calculated from CD spectra, and the prevalence of the beta-structure (85%) was shown. An irreversible conformational transition in the range 55-60 degrees C was found, which reduces the binding activity of cyprein in interaction with carcinoembryonic antigen (CEA) and anti-cyprein antibodies.

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Temperature-, ionic strength-, calcium ion- and pH-dependence of spatial structure of crustacin have been studied using CD and fluorescent spectroscopy. Secondary structure of crustacin was estimated by CD spectra. An irreversible conformational transition of crustacin's protein moiety connected with the loss of CEA-binding activity has been found at ca.

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Antigenic determinants of carcino-embryonic antigen (CEA) were spatially located using N-bromosuccinimide modification of tryptophan residues both in native (acetate buffer solution) and unfolded (guanidinium chloride solution) molecule of the antigen. Modification of exposed tryptophan residues failed to alter CEA antigenic activity and conformation of its protein portion as shown by CD spectroscopy. On the contrary, modification of buried tryptophan residues induced conformational changes of CEA protein portion connected with a considerable loss of its antigenic activity.

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Effects of temperature and pH on the spatial structures of trophoblast-specific beta 1-glycoprotein (TSG) and its various derivatives and fragments have been studied by circular dichroic spectroscopy. The spatial organization of the protein portion of TSG derivatives, as revealed by the spectroscopic evidence, has been discussed with respect to the antigenic activity of the species studied. We concluded that the TSG protein portion consists mainly of a beta-structural type.

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Spatial localization of antigenic determinants of trophoblast-specific beta I-glycoprotein (TSG) has been elucidated using chemical modifications of the sugar and protein moieties of the molecule. Various deglycosylation procedures of TSG afforded fragments slightly soluble even in the presence of powerful detergents. Treatment of TSG with boric acid and its salts, accompanied with a conformational change of the sugar moiety, failed to alter conformation of the protein portion as evidenced by CD spectral data.

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Temperature- and pH-dependence of spatial structure of a native trophoblast-specific beta-glycoprotein (TSG), its desialated and deglycosylated derivatives, as well as of a fragment obtained by partial acid hydrolysis on the temperature and pH variations has been studied using CD and UV spectroscopy. Within the range 45-50 degrees C a conformational transition of the protein moiety of TSG, leading to partially reversible alterations in tertiary and secondary structures of this glycoprotein after cooling the solution to 20 degrees C has been found out. The results of spectral studies of the spatial structure of the TSG protein component have been compared with the data on antigen activity of native, temperature- and pH-denaturated, desialated, and deglycosilated TSG.

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The spatial structure features of intact and deglycosylated carcino-embryonic antigen (CEA) have been studied by circular dichroism. Raman and UV-spectroscopy methods in order to elucidate a pattern and localization of CEA immunodominants. The temperature-induced changes in the spatial structure of the protein moiety were compared with data on the CEA immunochemical activity estimated by EIA procedure.

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