Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1021/acs.jpcb.0c04317 http://scihub22266oqcxt.onion/10.1021/acs.jpcb.0c04317 32551652!7341686!32551652     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=32551652&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Phys+Chem+B 2020 ; 124 (28): 5907-5912 Nephropedia Template TP {{tp|p=32551652|t=2020. Critical Differences between the Binding Features of the Spike Proteins of SARS-CoV-2 and SARS-CoV |pdf=|usr=}}{{32551652}} gab.com Text Critical Differences between the Binding Features of the Spike Proteins of SARS-CoV-2 and SARS-CoV JO: J Phys Chem B http://www.kidney.de/pget.php?&tw=1&pmid=32551652 #FOAvip The COVID-19 caused by SARS-CoV-2 has spread globally and caused tremendous loss of lives and properties, and it is of utmost urgency to understand its propagation process and to find ways to slow down the epidemic. In this work, we used a coarse-grained model to calculate the binding free energy of SARS-CoV-2 or SARS-CoV to their human receptor ACE2. The investigation of the free energy contribution of the interacting residues indicates that the residues located outside the receptor binding domain are the source of the stronger binding of the novel virus. Thus, the current results suggest that the essential evolution of SARS-CoV-2 happens remotely from the binding domain at the spike protein trimeric body. Such evolution may facilitate the conformational change and the infection process that occurs after the virus is bound to ACE2. By studying the binding pattern between SARS-CoV antibody m396 and SARS-CoV-2, it is found that the remote energetic contribution is missing, which might explain the absence of cross-reactivity of such antibodies. Twit Text FOAVip Critical Differences between the Binding Features of the Spike Proteins of SARS-CoV-2 and SARS-CoV ????J Phys Chem B http://www.kidney.de/pget.php?&tw=1&pmid=32551652 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32551652 #FOAvip English Wikipedia <ref>{{Cite pmid|32551652}}</ref> Critical Differences between the Binding Features of the Spike Proteins of SARS-CoV-2 and SARS-CoV #MMPMID32551652 Bai C; Warshel A J Phys Chem B 2020[Jul]; 124 (28): 5907-5912 PMID32551652show ga The COVID-19 caused by SARS-CoV-2 has spread globally and caused tremendous loss of lives and properties, and it is of utmost urgency to understand its propagation process and to find ways to slow down the epidemic. In this work, we used a coarse-grained model to calculate the binding free energy of SARS-CoV-2 or SARS-CoV to their human receptor ACE2. The investigation of the free energy contribution of the interacting residues indicates that the residues located outside the receptor binding domain are the source of the stronger binding of the novel virus. Thus, the current results suggest that the essential evolution of SARS-CoV-2 happens remotely from the binding domain at the spike protein trimeric body. Such evolution may facilitate the conformational change and the infection process that occurs after the virus is bound to ACE2. By studying the binding pattern between SARS-CoV antibody m396 and SARS-CoV-2, it is found that the remote energetic contribution is missing, which might explain the absence of cross-reactivity of such antibodies. |*Betacoronavirus/chemistry[MESH] |*Severe acute respiratory syndrome-related coronavirus/chemistry/immunology[MESH] |Angiotensin-Converting Enzyme 2[MESH] |Antibodies, Viral/chemistry[MESH] |Binding Sites[MESH] |Humans[MESH] |Molecular Dynamics Simulation[MESH] |Peptidyl-Dipeptidase A/chemistry[MESH] |Protein Binding[MESH] |SARS-CoV-2[MESH] |Spike Glycoprotein, Coronavirus/*chemistry[MESH]Critical Differences between the Binding Features of the Spike Protein(epmc).pdf DeepDyve Pubget Overpricing