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10.1039/d0nr03969a http://scihub22266oqcxt.onion/10.1039/d0nr03969a 32725017!ä!32725017 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 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       Nanoscale 2020 ; 12 (31): 16409-16413 Nephropedia Template TP {{tp|p=32725017|t=2020. Quantitative determination of mechanical stability in the novel coronavirus spike protein |pdf=|usr=}}{{32725017}} gab.com Text Quantitative determination of mechanical stability in the novel coronavirus spike protein JO: Nanoscale http://www.kidney.de/pget.php?&tw=1&pmid=32725017 #FOAvip We report on the novel observation about the gain in nanomechanical stability of the SARS-CoV-2 (CoV2) spike (S) protein in comparison with SARS-CoV from 2002 (CoV1). Our findings have several biological implications in the subfamily of coronaviruses, as they suggest that the receptor binding domain (RBD) ( approximately 200 amino acids) plays a fundamental role as a damping element of the massive viral particle's motion prior to cell-recognition, while also facilitating viral attachment, fusion and entry. The mechanical stability via pulling of the RBD is 250 pN and 200 pN for CoV2 and CoV1 respectively, and the additional stability observed for CoV2 ( approximately 50 pN) might play a role in the increasing spread of COVID-19. Twit Text FOAVip Quantitative determination of mechanical stability in the novel coronavirus spike protein ????Nanoscale http://www.kidney.de/pget.php?&tw=1&pmid=32725017 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32725017 #FOAvip English Wikipedia <ref>{{Cite pmid|32725017}}</ref> Quantitative determination of mechanical stability in the novel coronavirus spike protein #MMPMID32725017 Moreira RA; Chwastyk M; Baker JL; Guzman HV; Poma AB Nanoscale 2020[Aug]; 12 (31): 16409-16413 PMID32725017show ga We report on the novel observation about the gain in nanomechanical stability of the SARS-CoV-2 (CoV2) spike (S) protein in comparison with SARS-CoV from 2002 (CoV1). Our findings have several biological implications in the subfamily of coronaviruses, as they suggest that the receptor binding domain (RBD) ( approximately 200 amino acids) plays a fundamental role as a damping element of the massive viral particle's motion prior to cell-recognition, while also facilitating viral attachment, fusion and entry. The mechanical stability via pulling of the RBD is 250 pN and 200 pN for CoV2 and CoV1 respectively, and the additional stability observed for CoV2 ( approximately 50 pN) might play a role in the increasing spread of COVID-19. |Amino Acid Sequence[MESH] |Angiotensin-Converting Enzyme 2[MESH] |Betacoronavirus/*chemistry[MESH] |Binding Sites[MESH] |Humans[MESH] |Molecular Dynamics Simulation[MESH] |Peptidyl-Dipeptidase A/metabolism[MESH] |Protein Binding[MESH] |Protein Domains[MESH] |Protein Stability[MESH] |SARS-CoV-2[MESH] |Severe acute respiratory syndrome-related coronavirus/chemistry[MESH] |Species Specificity[MESH]Quantitative determination of mechanical stability in the novel corona(epmc).pdf DeepDyve Pubget Overpricing