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10.1038/s41467-021-21953-3 http://scihub22266oqcxt.onion/10.1038/s41467-021-21953-3 33782395!8007728!33782395     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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\33782395.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Nat+Commun 2021 ; 12 (1): 1936 Nephropedia Template TP {{tp|p=33782395|t=2021. The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase separates with RNA |pdf=|usr=}}{{33782395}} gab.com Text The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase separates with RNA JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=33782395 #FOAvip The SARS-CoV-2 nucleocapsid (N) protein is an abundant RNA-binding protein critical for viral genome packaging, yet the molecular details that underlie this process are poorly understood. Here we combine single-molecule spectroscopy with all-atom simulations to uncover the molecular details that contribute to N protein function. N protein contains three dynamic disordered regions that house putative transiently-helical binding motifs. The two folded domains interact minimally such that full-length N protein is a flexible and multivalent RNA-binding protein. N protein also undergoes liquid-liquid phase separation when mixed with RNA, and polymer theory predicts that the same multivalent interactions that drive phase separation also engender RNA compaction. We offer a simple symmetry-breaking model that provides a plausible route through which single-genome condensation preferentially occurs over phase separation, suggesting that phase separation offers a convenient macroscopic readout of a key nanoscopic interaction. Twit Text FOAVip The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase separates with RNA ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=33782395 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33782395 #FOAvip English Wikipedia <ref>{{Cite pmid|33782395}}</ref> The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase separates with RNA #MMPMID33782395 Cubuk J; Alston JJ; Incicco JJ; Singh S; Stuchell-Brereton MD; Ward MD; Zimmerman MI; Vithani N; Griffith D; Wagoner JA; Bowman GR; Hall KB; Soranno A; Holehouse AS Nat Commun 2021[Mar]; 12 (1): 1936 PMID33782395show ga The SARS-CoV-2 nucleocapsid (N) protein is an abundant RNA-binding protein critical for viral genome packaging, yet the molecular details that underlie this process are poorly understood. Here we combine single-molecule spectroscopy with all-atom simulations to uncover the molecular details that contribute to N protein function. N protein contains three dynamic disordered regions that house putative transiently-helical binding motifs. The two folded domains interact minimally such that full-length N protein is a flexible and multivalent RNA-binding protein. N protein also undergoes liquid-liquid phase separation when mixed with RNA, and polymer theory predicts that the same multivalent interactions that drive phase separation also engender RNA compaction. We offer a simple symmetry-breaking model that provides a plausible route through which single-genome condensation preferentially occurs over phase separation, suggesting that phase separation offers a convenient macroscopic readout of a key nanoscopic interaction. |Binding Sites[MESH] |COVID-19/virology[MESH] |Coronavirus Nucleocapsid Proteins/*chemistry/*metabolism[MESH] |Dimerization[MESH] |Molecular Dynamics Simulation[MESH] |Phosphoproteins/chemistry/metabolism[MESH] |Protein Conformation[MESH] |Protein Domains[MESH] |RNA, Viral/*chemistry/*metabolism[MESH]The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase (epmc).pdf DeepDyve Pubget Overpricing