Performed stereochemical analysis of possible spatial arrangements for human involucrin having amino acid sequence with tandem repeats. Based on this analysis and summarized experimental data, a structural model of involucrin was formulated. The model suggests the sites and modes of interaction of involucrin with small proline-rich proteins of the skin. A paper on the structural model was published. Performed amino acid sequence analysis of bacterial proteins having arrays of tandem repeats. Based on this analysis and molecular modeling, a beta-helix model was suggested for the filamentous hemagglutinin adhesin of Bordetella pertussis and related bacterial secretory proteins. A manuscript is submitted for publication. Performed inspection of the known solenoid-like structures of proteins. These proteins were classified and the relationships between their sequences, structure and function has been reviewed. A paper is in press. Performed amino acid sequence analysis of signal peptides and regions adjacent to them in order to understand the mechanism of protein translocation across the cytoplasmic membrane. Established that the net charge of the first 18 residues of the mature sequence is essential for protein translocation of gram-negative bacteria. A paper was published. A short coiled-coil peptide with the potential to self-assemble into long fibrils have been designed, synthesized and analyzed. A manuscript is submitted. Performed amino acid sequence analysis and molecular modeling of several newly cloned of sea urchin proteins. Established that these proteins have sequence similarity to C1q complement factor, a protein with the known 3D structure. This suggests an oligomerization state, cellular locations and possible function of these proteins.
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