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How Similar Are Proteins and Origami?

Protein folding and structural biology are highly active disciplines that combine basic research in various fields, including biology, chemistry, physics, and computer science, with practical applications in biomedicine and nanotechnology. However, there are still gaps in the understanding of the de...

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Detalles Bibliográficos
Autores principales: Azulay, Hay, Lutaty, Aviv, Qvit, Nir
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9138822/
https://www.ncbi.nlm.nih.gov/pubmed/35625549
http://dx.doi.org/10.3390/biom12050622
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author Azulay, Hay
Lutaty, Aviv
Qvit, Nir
author_facet Azulay, Hay
Lutaty, Aviv
Qvit, Nir
author_sort Azulay, Hay
collection PubMed
description Protein folding and structural biology are highly active disciplines that combine basic research in various fields, including biology, chemistry, physics, and computer science, with practical applications in biomedicine and nanotechnology. However, there are still gaps in the understanding of the detailed mechanisms of protein folding, and protein structure-function relations. In an effort to bridge these gaps, this paper studies the equivalence of proteins and origami. Research on proteins and origami provides strong evidence to support the use of origami folding principles and mechanical models to explain aspects of proteins formation and function. Although not identical, the equivalence of origami and proteins emerges in: (i) the folding processes, (ii) the shape and structure of proteins and origami models, and (iii) the intrinsic mechanical properties of the folded structures/models, which allows them to synchronically fold/unfold and effectively distribute forces to the whole structure. As a result, origami can contribute to the understanding of various key protein-related mechanisms and support the design of de novo proteins and nanomaterials.
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spelling pubmed-91388222022-05-28 How Similar Are Proteins and Origami? Azulay, Hay Lutaty, Aviv Qvit, Nir Biomolecules Article Protein folding and structural biology are highly active disciplines that combine basic research in various fields, including biology, chemistry, physics, and computer science, with practical applications in biomedicine and nanotechnology. However, there are still gaps in the understanding of the detailed mechanisms of protein folding, and protein structure-function relations. In an effort to bridge these gaps, this paper studies the equivalence of proteins and origami. Research on proteins and origami provides strong evidence to support the use of origami folding principles and mechanical models to explain aspects of proteins formation and function. Although not identical, the equivalence of origami and proteins emerges in: (i) the folding processes, (ii) the shape and structure of proteins and origami models, and (iii) the intrinsic mechanical properties of the folded structures/models, which allows them to synchronically fold/unfold and effectively distribute forces to the whole structure. As a result, origami can contribute to the understanding of various key protein-related mechanisms and support the design of de novo proteins and nanomaterials. MDPI 2022-04-21 /pmc/articles/PMC9138822/ /pubmed/35625549 http://dx.doi.org/10.3390/biom12050622 Text en © 2022 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
Azulay, Hay
Lutaty, Aviv
Qvit, Nir
How Similar Are Proteins and Origami?
title How Similar Are Proteins and Origami?
title_full How Similar Are Proteins and Origami?
title_fullStr How Similar Are Proteins and Origami?
title_full_unstemmed How Similar Are Proteins and Origami?
title_short How Similar Are Proteins and Origami?
title_sort how similar are proteins and origami?
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9138822/
https://www.ncbi.nlm.nih.gov/pubmed/35625549
http://dx.doi.org/10.3390/biom12050622
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