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10.1002/gch2.202000067 http://scihub22266oqcxt.onion/10.1002/gch2.202000067 33173592!7646041!33173592     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Glob+Chall 2020 ; 4 (12): 2000067 Nephropedia Template TP {{tp|p=33173592|t=2020. A Hydrophobic-Interaction-Based Mechanism Triggers Docking between the SARS-CoV-2 Spike and Angiotensin-Converting Enzyme 2 |pdf=|usr=}}{{33173592}} gab.com Text A Hydrophobic-Interaction-Based Mechanism Triggers Docking between the SARS-CoV-2 Spike and Angiotensin-Converting Enzyme 2 JO: Glob Chall http://www.kidney.de/pget.php?&tw=1&pmid=33173592 #FOAvip A recent experimental study found that the binding affinity between the cellular receptor human angiotensin-converting enzyme 2 (ACE2) and receptor-binding domain (RBD) in the spike (S) protein of novel severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is more than tenfold higher than that of the original severe acute respiratory syndrome coronavirus (SARS-CoV). However, main chain structures of the SARS-CoV-2 RBD are almost the same with that of the SARS-CoV RBD. Understanding the physical mechanism responsible for the outstanding affinity between the SARS-CoV-2 S and ACE2 is an "urgent challenge" for developing blockers, vaccines, and therapeutic antibodies against the coronavirus disease 2019 (COVID-19) pandemic. Taking into account the mechanisms of hydrophobic interaction, hydration shell, surface tension, and the shielding effect of water molecules, this study reveals a hydrophobic-interaction-based mechanism by means of which SARS-CoV-2 S and ACE2 bind together in an aqueous environment. The hydrophobic interaction between the SARS-CoV-2 S and ACE2 protein is found to be significantly greater than that between SARS-CoV S and ACE2. At the docking site, the hydrophobic portions of the hydrophilic side chains of SARS-CoV-2 S are found to be involved in the hydrophobic interaction between SARS-CoV-2 S and ACE2. Twit Text FOAVip A Hydrophobic-Interaction-Based Mechanism Triggers Docking between the SARS-CoV-2 Spike and Angiotensin-Converting Enzyme 2 ????Glob Chall http://www.kidney.de/pget.php?&tw=1&pmid=33173592 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33173592 #FOAvip English Wikipedia <ref>{{Cite pmid|33173592}}</ref> A Hydrophobic-Interaction-Based Mechanism Triggers Docking between the SARS-CoV-2 Spike and Angiotensin-Converting Enzyme 2 #MMPMID33173592 Li J; Ma X; Guo S; Hou C; Shi L; Zhang H; Zheng B; Liao C; Yang L; Ye L; He X Glob Chall 2020[Dec]; 4 (12): 2000067 PMID33173592show ga A recent experimental study found that the binding affinity between the cellular receptor human angiotensin-converting enzyme 2 (ACE2) and receptor-binding domain (RBD) in the spike (S) protein of novel severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is more than tenfold higher than that of the original severe acute respiratory syndrome coronavirus (SARS-CoV). However, main chain structures of the SARS-CoV-2 RBD are almost the same with that of the SARS-CoV RBD. Understanding the physical mechanism responsible for the outstanding affinity between the SARS-CoV-2 S and ACE2 is an "urgent challenge" for developing blockers, vaccines, and therapeutic antibodies against the coronavirus disease 2019 (COVID-19) pandemic. Taking into account the mechanisms of hydrophobic interaction, hydration shell, surface tension, and the shielding effect of water molecules, this study reveals a hydrophobic-interaction-based mechanism by means of which SARS-CoV-2 S and ACE2 bind together in an aqueous environment. The hydrophobic interaction between the SARS-CoV-2 S and ACE2 protein is found to be significantly greater than that between SARS-CoV S and ACE2. At the docking site, the hydrophobic portions of the hydrophilic side chains of SARS-CoV-2 S are found to be involved in the hydrophobic interaction between SARS-CoV-2 S and ACE2. äA Hydrophobic-Interaction-Based Mechanism Triggers Docking between the(epmc).pdf DeepDyve Pubget Overpricing