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10.3934/mbe.2021120 http://scihub22266oqcxt.onion/10.3934/mbe.2021120 33892550!8279046!33892550     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Math+Biosci+Eng 2021 ; 18 (3): 2372-2383 Nephropedia Template TP {{tp|p=33892550|t=2021. Electrostatic features for nucleocapsid proteins of SARS-CoV and SARS-CoV-2 |pdf=|usr=}}{{33892550}} gab.com Text Electrostatic features for nucleocapsid proteins of SARS-CoV and SARS-CoV-2 JO: Math Biosci Eng http://www.kidney.de/pget.php?&tw=1&pmid=33892550 #FOAvip 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. Twit Text FOAVip Electrostatic features for nucleocapsid proteins of SARS-CoV and SARS-CoV-2 ????Math Biosci Eng http://www.kidney.de/pget.php?&tw=1&pmid=33892550 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33892550 #FOAvip English Wikipedia <ref>{{Cite pmid|33892550}}</ref> Electrostatic features for nucleocapsid proteins of SARS-CoV and SARS-CoV-2 #MMPMID33892550 Guo W; Xie Y; E Lopez-Hernandez A; Sun S; Li L Math Biosci Eng 2021[Mar]; 18 (3): 2372-2383 PMID33892550show ga 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. |*COVID-19[MESH] |*Nucleocapsid Proteins[MESH] |Humans[MESH] |SARS-CoV-2[MESH]Electrostatic features for nucleocapsid proteins of SARS-CoV and SARS-(epmc).pdf DeepDyve Pubget Overpricing