The prerequisites for the presented research were the works in which the system regularity of the chirality sign change in the transition to a higher level of structural and functional organization in proteins and nucleic acids (V.A. Tverdislov et al., 2012, 2017) was revealed. A new approach to the evaluation of the sign of chirality (helicity and supercoiling) in the structural hierarchy of proteins is proposed. An analysis of the mutual arrangement of α-carbon atoms was carried out to determine the sign and magnitude of the chirality of the secondary and tertiary structure of proteins . The angle between the vector of the direction of the helix and the vector of the sum of vector products makes it possible to uniquely identify the direction of rotation of the helix in the molecule. A method for constructing "chirality maps" which clearly demonstrates the areas corresponding to a narrow range of the possible angle for the two types of secondary spiral structure is proposed.
proteins, chirality, enantiomers, alpha-carbon atom, right-handed alpha helix, left-handed polyproline helix, cross product, direction vector, chirality map
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