Russian Academy of Sciences Siberian Branch Institute of Cytology and Genetics Laboratory of Theoretical Genetics Proceedings of the Second International Conference on Bioinformatics of Genome Regulation and Structure

The purpose of the work was to investigate at the molecular structural and energy levels the consequence ofamino acid substitutions in collagen that cause systemic diseases. The data have been systematized on defectsin human collagen III, and the patterns of single-nucleotide polymorphisms collected; then molecular mechanicscalculations were performed for native and mutant collagen molecule fragments. The observed energycomponents and structural alterations that accompany particular amino acid substitutions were used to proposean interpretation of negative consequences in terms of stability and hydration of the macromolecule.This work was supported by the Russian Foundation for Basic Research (grant 98-04-48755). ELUCIDATION OF THE STRUCTURE OF WHOLE PROTEIN:HUMAN COLLAGEN III Milchevsky Ju.V., Zorov B.S., Esipova N.G., Tumanyan V.G. Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 32 Vavilov str., Moscow,117984 Russia