In the present study, various approaches to the quantitation of the molecular chirality, one of the pressing problems of biochemical physics, are considered. A new relatively simple method for estimating chirality in protein secondary structures is proposed. The method is based on defining the reference (control) points - alpha-carbon atoms in the polypeptide chain followed by calculating the mixed products of bond vectors associated with relative position of these points. Special attention was given to the normalization of chirality in protein helical structures. We analyzed 983 proteins of 12 classes taken from the PDB database. Along with energetically favorable right-handed α- and 310-helixes, the secondary structure motifs in the left-handed conformation were found. Based on the developed method a chirality map of protein helical structures was obtained. This method can be considered as a step towards extending the concept of chirality to hierarchically higher categories of objects - protein globules and supramolecular structures.
proteins, chirality, alpha-carbon, α-helix, 310-helix, chirality map
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