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Flexible Folding: Disulfide-Containing Peptides and Proteins Choose the Pathway Depending on the Environments
In the last few decades, development of novel experimental techniques, such as new types of disulfide (SS)-forming reagents and genetic and chemical technologies for synthesizing designed artificial proteins, is opening a new realm of the oxidative folding study where peptides and proteins can be fo...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7794709/ https://www.ncbi.nlm.nih.gov/pubmed/33401729 http://dx.doi.org/10.3390/molecules26010195 |
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author | Arai, Kenta Iwaoka, Michio |
author_facet | Arai, Kenta Iwaoka, Michio |
author_sort | Arai, Kenta |
collection | PubMed |
description | In the last few decades, development of novel experimental techniques, such as new types of disulfide (SS)-forming reagents and genetic and chemical technologies for synthesizing designed artificial proteins, is opening a new realm of the oxidative folding study where peptides and proteins can be folded under physiologically more relevant conditions. In this review, after a brief overview of the historical and physicochemical background of oxidative protein folding study, recently revealed folding pathways of several representative peptides and proteins are summarized, including those having two, three, or four SS bonds in the native state, as well as those with odd Cys residues or consisting of two peptide chains. Comparison of the updated pathways with those reported in the early years has revealed the flexible nature of the protein folding pathways. The significantly different pathways characterized for hen-egg white lysozyme and bovine milk α-lactalbumin, which belong to the same protein superfamily, suggest that the information of protein folding pathways, not only the native folded structure, is encoded in the amino acid sequence. The application of the flexible pathways of peptides and proteins to the engineering of folded three-dimensional structures is an interesting and important issue in the new realm of the current oxidative protein folding study. |
format | Online Article Text |
id | pubmed-7794709 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-77947092021-01-10 Flexible Folding: Disulfide-Containing Peptides and Proteins Choose the Pathway Depending on the Environments Arai, Kenta Iwaoka, Michio Molecules Review In the last few decades, development of novel experimental techniques, such as new types of disulfide (SS)-forming reagents and genetic and chemical technologies for synthesizing designed artificial proteins, is opening a new realm of the oxidative folding study where peptides and proteins can be folded under physiologically more relevant conditions. In this review, after a brief overview of the historical and physicochemical background of oxidative protein folding study, recently revealed folding pathways of several representative peptides and proteins are summarized, including those having two, three, or four SS bonds in the native state, as well as those with odd Cys residues or consisting of two peptide chains. Comparison of the updated pathways with those reported in the early years has revealed the flexible nature of the protein folding pathways. The significantly different pathways characterized for hen-egg white lysozyme and bovine milk α-lactalbumin, which belong to the same protein superfamily, suggest that the information of protein folding pathways, not only the native folded structure, is encoded in the amino acid sequence. The application of the flexible pathways of peptides and proteins to the engineering of folded three-dimensional structures is an interesting and important issue in the new realm of the current oxidative protein folding study. MDPI 2021-01-02 /pmc/articles/PMC7794709/ /pubmed/33401729 http://dx.doi.org/10.3390/molecules26010195 Text en © 2021 by the authors. 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 (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Arai, Kenta Iwaoka, Michio Flexible Folding: Disulfide-Containing Peptides and Proteins Choose the Pathway Depending on the Environments |
title | Flexible Folding: Disulfide-Containing Peptides and Proteins Choose the Pathway Depending on the Environments |
title_full | Flexible Folding: Disulfide-Containing Peptides and Proteins Choose the Pathway Depending on the Environments |
title_fullStr | Flexible Folding: Disulfide-Containing Peptides and Proteins Choose the Pathway Depending on the Environments |
title_full_unstemmed | Flexible Folding: Disulfide-Containing Peptides and Proteins Choose the Pathway Depending on the Environments |
title_short | Flexible Folding: Disulfide-Containing Peptides and Proteins Choose the Pathway Depending on the Environments |
title_sort | flexible folding: disulfide-containing peptides and proteins choose the pathway depending on the environments |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7794709/ https://www.ncbi.nlm.nih.gov/pubmed/33401729 http://dx.doi.org/10.3390/molecules26010195 |
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