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10.1016/j.isci.2021.102523 http://scihub22266oqcxt.onion/10.1016/j.isci.2021.102523 33997662!8103780!33997662     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       iScience 2021 ; 24 (6): 102523 Nephropedia Template TP {{tp|p=33997662|t=2021. Energetic and structural features of SARS-CoV-2 N-protein co-assemblies with nucleic acids |pdf=|usr=}}{{33997662}} gab.com Text Energetic and structural features of SARS-CoV-2 N-protein co-assemblies with nucleic acids JO: iScience http://www.kidney.de/pget.php?&tw=1&pmid=33997662 #FOAvip Nucleocapsid (N) protein of the SARS-CoV-2 virus packages the viral genome into well-defined ribonucleoprotein particles, but the molecular pathway is still unclear. N-protein is dimeric and consists of two folded domains with nucleic acid (NA) binding sites, surrounded by intrinsically disordered regions that promote liquid-liquid phase separation. Here, we use biophysical tools to study N-protein interactions with oligonucleotides of different lengths, examining the size, composition, secondary structure, and energetics of the resulting states. We observe the formation of supramolecular clusters or nuclei preceding growth into phase-separated droplets. Short hexanucleotide NA forms compact 2:2 N-protein/NA complexes with reduced disorder. Longer oligonucleotides expose additional N-protein interactions and multi-valent protein-NA interactions, which generate higher-order mixed oligomers and simultaneously promote growth of droplets. Phase separation is accompanied by a significant change in protein secondary structure, different from that caused by initial NA binding, which may contribute to the assembly of ribonucleoprotein particles within macromolecular condensates. Twit Text FOAVip Energetic and structural features of SARS-CoV-2 N-protein co-assemblies with nucleic acids ????iScience http://www.kidney.de/pget.php?&tw=1&pmid=33997662 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33997662 #FOAvip English Wikipedia <ref>{{Cite pmid|33997662}}</ref> Energetic and structural features of SARS-CoV-2 N-protein co-assemblies with nucleic acids #MMPMID33997662 Zhao H; Wu D; Nguyen A; Li Y; Adao RC; Valkov E; Patterson GH; Piszczek G; Schuck P iScience 2021[Jun]; 24 (6): 102523 PMID33997662show ga Nucleocapsid (N) protein of the SARS-CoV-2 virus packages the viral genome into well-defined ribonucleoprotein particles, but the molecular pathway is still unclear. N-protein is dimeric and consists of two folded domains with nucleic acid (NA) binding sites, surrounded by intrinsically disordered regions that promote liquid-liquid phase separation. Here, we use biophysical tools to study N-protein interactions with oligonucleotides of different lengths, examining the size, composition, secondary structure, and energetics of the resulting states. We observe the formation of supramolecular clusters or nuclei preceding growth into phase-separated droplets. Short hexanucleotide NA forms compact 2:2 N-protein/NA complexes with reduced disorder. Longer oligonucleotides expose additional N-protein interactions and multi-valent protein-NA interactions, which generate higher-order mixed oligomers and simultaneously promote growth of droplets. Phase separation is accompanied by a significant change in protein secondary structure, different from that caused by initial NA binding, which may contribute to the assembly of ribonucleoprotein particles within macromolecular condensates. äEnergetic and structural features of SARS-CoV-2 N-protein co-assemblie(epmc).pdf DeepDyve Pubget Overpricing