MODELLING OF THE INDIVIDUAL STRUCTURAL TEMPLATE OF PROTEIN ON DETERMINING IT NUCLEOTIDE SEQUENCES
SI « Institute of neurology, psychiatry and narcology of the AMSU», Kharkov, Ukraine
Key words: a configuration of peptide bond, genetic code of spatial structure of protein, personal structural templates of major actin and ?-actin 1
Motivation and Aim: The novel way of modeling of spatial structure of protein on determining it nucleotide sequences is elaborated. On analogies with rotamers on C—C ?-bound a concept configurations of peptide bound (CPB) is entered as basic element three-dimensional structure of protein, encoded in a genome along with amino acid.
Methods and Algorithms: On ringlateral models of polyalanine it is shown, those three discrete variant configurations of peptide bound (R, 0 and L) determine three different second structures of polypeptide chain: the right spiral, the ?-strand and the left spiral. On the basis of the empirical table of a composite genetic  code the author of the given research had been made the ^ . The important advantage of a method is that it is possible to construct a structural pattern individually for any unknown protein only "having read through" determining it nucleotide sequence in according with the table of a genetic code of spatial structure of protein, and also to decode presence and position of fragments of secondary structure of it.
Results: In this worker were modeled a structural templates of two homologues major actin and ?-actin 1. Its visualized is possible in the graphic editor Ggenedit.exe.
Conclusion: Thus, two homologous proteins (the major actin and ?-actin 1) the identical size (375 а.a.) with identity degree amino acid sequences of 91 % are characterized only 35 % of similarity of sequences of a CPB. It means that such homologues possess various three-dimensional structures and about any general template for its modeling of speech cannot go.
1. /3D Modelling Tutorial for Poser 7.pdf
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