A Method for Calculating the Sign and Degree of Chirality of Supercoiled Protein Structures

Abstract

Chirality plays an important role in studies of natural protein structures. Therefore, much attention is paid to solving the problems associated with the development of criteria and methods for assessing the chirality of biomolecules. In this paper, a new method for calculating the sign and degree of chirality of superhelices is proposed. The method makes it possible to characterize the chirality sign and to quantify coiled-coils and collagen superhelices. The degree of chirality is understood as a value indicating the intensity of twisting of individual helices around the axis of the superhelix. The calculation requires information about the relative spatial arrangement of the alpha carbon of the amino acid residues of the helices that make up the superhelix. The use of a small amount of raw data makes the method easy to apply, and the validity of the results of this study is confirmed through the analysis of real protein structures.