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Updated: Oct 9, 2025

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Quantitative Assessment of Chirality of Protein Secondary Structures and Phenylalanine Peptide Nanotubes
Alla Sidorova1, Vladimir Bystrov2, Aleksey Lutsenko1
1Faculty of Physics, Lomonosov Moscow State University, 119991 Moscow, Russia.
Abstract:
In this study we consider the features of spatial-structure formation in proteins and their application in bioengineering. Methods for the quantitative assessment of the chirality of regular helical and irregular structures of proteins are presented. The features of self-assembly of phenylalanine (F) into peptide nanotubes (PNT), which form helices of different chirality, are also analyzed. A method is proposed for calculating the magnitude and sign of the chirality of helix-like peptide nanotubes using a sequence of vectors for the dipole moments of individual peptides.
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