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Methods to Determine the Chirality Sign for Helical and Superhelical Protein Structures

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Abstract

A method was designed to describe the helical structures of various levels of organization in proteins. The method makes it possible to characterize the sign of chirality/helicity and to quantify α-helices, 310-helices, and coiled-coil structures. The data is important for developing the earlier concept of sign-alternating chiral hierarchies of nucleic acid and protein structures. A sufficient condition for the method is the relative location of α-carbons in the helix. With this condition satisfied, the amount of information to be processed can be reduced by one order of magnitude. The method thus offers a clear benefit for processing large data sets.

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Funding

This work was supported by the Basic and Applied Space Research Interdisciplinary Research-and-Education School (Moscow State University) and the Russian Science Foundation (project no. 19-74-00082).

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Authors and Affiliations

  1. Department of Physics, Moscow State University, 119991, Moscow, Russia

    A. E. Sidorova, A. O. Lutsenko, D. K. Shpigun, E. V. Malyshko & V. A. Tverdislov

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  1. A. E. Sidorova
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  2. A. O. Lutsenko
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  3. D. K. Shpigun
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  4. E. V. Malyshko
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  5. V. A. Tverdislov
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Correspondence to A. E. Sidorova.

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Translated by T. Tkacheva

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Sidorova, A.E., Lutsenko, A.O., Shpigun, D.K. et al. Methods to Determine the Chirality Sign for Helical and Superhelical Protein Structures. BIOPHYSICS 66, 357–363 (2021). https://doi.org/10.1134/S0006350921030180

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  • DOI: https://doi.org/10.1134/S0006350921030180

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