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Electrostatic features for nucleocapsid proteins of SARS-CoV and SARS-CoV-2
COVID-19 is increasingly affecting human health and global economy. Understanding the fundamental mechanisms of Severe Acute Respiratory Syndrome CoronaVirus 2 (SARS-CoV-2) is highly demanded to develop treatments for COVID-19. SARS-CoV and SARS-CoV-2 share 92.06% identity in their N protein RBDs’ s...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8279046/ https://www.ncbi.nlm.nih.gov/pubmed/33892550 http://dx.doi.org/10.3934/mbe.2021120 |
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author | Guo, Wenhan Xie, Yixin Lopez-Hernandez, Alan E Sun, Shengjie Li, Lin |
author_facet | Guo, Wenhan Xie, Yixin Lopez-Hernandez, Alan E Sun, Shengjie Li, Lin |
author_sort | Guo, Wenhan |
collection | PubMed |
description | COVID-19 is increasingly affecting human health and global economy. Understanding the fundamental mechanisms of Severe Acute Respiratory Syndrome CoronaVirus 2 (SARS-CoV-2) is highly demanded to develop treatments for COVID-19. SARS-CoV and SARS-CoV-2 share 92.06% identity in their N protein RBDs’ sequences, which results in very similar structures. However, the SARS-CoV-2 is more easily to spread. Utilizing multi-scale computational approaches, this work studied the fundamental mechanisms of the nucleocapsid (N) proteins of SARS-CoV and SARS-CoV-2, including their stabilities and binding strengths with RNAs at different pH values. Electrostatic potential on the surfaces of N proteins show that both the N proteins of SARS-CoV and SARS-CoV-2 have dominantly positive potential to attract RNAs. The binding forces between SARS-CoV N protein and RNAs at different distances are similar to that of SARS-CoV-2, both in directions and magnitudes. The electric filed lines between N proteins and RNAs are also similar for both SARS-CoV and SARS-CoV-2. The folding energy and binding energy dependence on pH revealed that the best environment for N proteins to perform their functions with RNAs is the weak acidic environment. |
format | Online Article Text |
id | pubmed-8279046 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
record_format | MEDLINE/PubMed |
spelling | pubmed-82790462021-07-14 Electrostatic features for nucleocapsid proteins of SARS-CoV and SARS-CoV-2 Guo, Wenhan Xie, Yixin Lopez-Hernandez, Alan E Sun, Shengjie Li, Lin Math Biosci Eng Article COVID-19 is increasingly affecting human health and global economy. Understanding the fundamental mechanisms of Severe Acute Respiratory Syndrome CoronaVirus 2 (SARS-CoV-2) is highly demanded to develop treatments for COVID-19. SARS-CoV and SARS-CoV-2 share 92.06% identity in their N protein RBDs’ sequences, which results in very similar structures. However, the SARS-CoV-2 is more easily to spread. Utilizing multi-scale computational approaches, this work studied the fundamental mechanisms of the nucleocapsid (N) proteins of SARS-CoV and SARS-CoV-2, including their stabilities and binding strengths with RNAs at different pH values. Electrostatic potential on the surfaces of N proteins show that both the N proteins of SARS-CoV and SARS-CoV-2 have dominantly positive potential to attract RNAs. The binding forces between SARS-CoV N protein and RNAs at different distances are similar to that of SARS-CoV-2, both in directions and magnitudes. The electric filed lines between N proteins and RNAs are also similar for both SARS-CoV and SARS-CoV-2. The folding energy and binding energy dependence on pH revealed that the best environment for N proteins to perform their functions with RNAs is the weak acidic environment. 2021-03-09 /pmc/articles/PMC8279046/ /pubmed/33892550 http://dx.doi.org/10.3934/mbe.2021120 Text en https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0 (https://creativecommons.org/licenses/by/4.0/) ) |
spellingShingle | Article Guo, Wenhan Xie, Yixin Lopez-Hernandez, Alan E Sun, Shengjie Li, Lin Electrostatic features for nucleocapsid proteins of SARS-CoV and SARS-CoV-2 |
title | Electrostatic features for nucleocapsid proteins of SARS-CoV and SARS-CoV-2 |
title_full | Electrostatic features for nucleocapsid proteins of SARS-CoV and SARS-CoV-2 |
title_fullStr | Electrostatic features for nucleocapsid proteins of SARS-CoV and SARS-CoV-2 |
title_full_unstemmed | Electrostatic features for nucleocapsid proteins of SARS-CoV and SARS-CoV-2 |
title_short | Electrostatic features for nucleocapsid proteins of SARS-CoV and SARS-CoV-2 |
title_sort | electrostatic features for nucleocapsid proteins of sars-cov and sars-cov-2 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8279046/ https://www.ncbi.nlm.nih.gov/pubmed/33892550 http://dx.doi.org/10.3934/mbe.2021120 |
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