Quantitative Assessment of Chirality of Protein Secondary Structures and Phenylalanine Peptide Nanotubes

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...

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Autores principales: Sidorova, Alla, Bystrov, Vladimir, Lutsenko, Aleksey, Shpigun, Denis, Belova, Ekaterina, Likhachev, Ilya
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8707344/
https://www.ncbi.nlm.nih.gov/pubmed/34947648
http://dx.doi.org/10.3390/nano11123299
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author Sidorova, Alla
Bystrov, Vladimir
Lutsenko, Aleksey
Shpigun, Denis
Belova, Ekaterina
Likhachev, Ilya
author_facet Sidorova, Alla
Bystrov, Vladimir
Lutsenko, Aleksey
Shpigun, Denis
Belova, Ekaterina
Likhachev, Ilya
author_sort Sidorova, Alla
collection PubMed
description 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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spelling pubmed-87073442021-12-25 Quantitative Assessment of Chirality of Protein Secondary Structures and Phenylalanine Peptide Nanotubes Sidorova, Alla Bystrov, Vladimir Lutsenko, Aleksey Shpigun, Denis Belova, Ekaterina Likhachev, Ilya Nanomaterials (Basel) Article 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. MDPI 2021-12-05 /pmc/articles/PMC8707344/ /pubmed/34947648 http://dx.doi.org/10.3390/nano11123299 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Sidorova, Alla
Bystrov, Vladimir
Lutsenko, Aleksey
Shpigun, Denis
Belova, Ekaterina
Likhachev, Ilya
Quantitative Assessment of Chirality of Protein Secondary Structures and Phenylalanine Peptide Nanotubes
title Quantitative Assessment of Chirality of Protein Secondary Structures and Phenylalanine Peptide Nanotubes
title_full Quantitative Assessment of Chirality of Protein Secondary Structures and Phenylalanine Peptide Nanotubes
title_fullStr Quantitative Assessment of Chirality of Protein Secondary Structures and Phenylalanine Peptide Nanotubes
title_full_unstemmed Quantitative Assessment of Chirality of Protein Secondary Structures and Phenylalanine Peptide Nanotubes
title_short Quantitative Assessment of Chirality of Protein Secondary Structures and Phenylalanine Peptide Nanotubes
title_sort quantitative assessment of chirality of protein secondary structures and phenylalanine peptide nanotubes
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8707344/
https://www.ncbi.nlm.nih.gov/pubmed/34947648
http://dx.doi.org/10.3390/nano11123299
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