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10.1007/s12104-020-09985-0 http://scihub22266oqcxt.onion/10.1007/s12104-020-09985-0 33219414!7678775!33219414     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=33219414&cmd=llinks): Failed to open stream: HTTP request failed! 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(1)H, (13)C, and (15)N backbone and side chain chemical shift assignments of the SARS-CoV-2 non-structural protein 7 |pdf=|usr=}}{{33219414}} gab.com Text (1)H, (13)C, and (15)N backbone and side chain chemical shift assignments of the SARS-CoV-2 non-structural protein 7 JO: Biomol NMR Assign http://www.kidney.de/pget.php?&tw=1&pmid=33219414 #FOAvip The SARS-CoV-2 genome encodes for approximately 30 proteins. Within the international project covid19-nmr, we distribute the spectroscopic analysis of the viral proteins and RNA. Here, we report NMR chemical shift assignments for the protein nsp7. The 83 amino acid nsp7 protein is an essential cofactor in the RNA-dependent RNA polymerase. The polymerase activity and processivity of nsp12 are greatly enhanced by binding 1 copy of nsp7 and 2 copies of nsp8 to form a 160 kD complex. A separate hexadecameric complex of nsp7 and nsp8 (8 copies of each) forms a large ring-like structure. Thus, nsp7 is an important component of several large protein complexes that are required for replication of the large and complex coronavirus genome. We here report the near-complete NMR backbone and sidechain resonance assignment ((1)H,(13)C,(15)N) of isolated nsp7 from SARS-CoV-2 in solution. Further, we derive the secondary structure and compare it to the previously reported assignments and structure of the SARS-CoV nsp7. Twit Text FOAVip (1)H, (13)C, and (15)N backbone and side chain chemical shift assignments of the SARS-CoV-2 non-structural protein 7 ????Biomol NMR Assign http://www.kidney.de/pget.php?&tw=1&pmid=33219414 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33219414 #FOAvip English Wikipedia <ref>{{Cite pmid|33219414}}</ref> (1)H, (13)C, and (15)N backbone and side chain chemical shift assignments of the SARS-CoV-2 non-structural protein 7 #MMPMID33219414 Tonelli M; Rienstra C; Anderson TK; Kirchdoerfer R; Henzler-Wildman K Biomol NMR Assign 2021[Apr]; 15 (1): 73-77 PMID33219414show ga The SARS-CoV-2 genome encodes for approximately 30 proteins. Within the international project covid19-nmr, we distribute the spectroscopic analysis of the viral proteins and RNA. Here, we report NMR chemical shift assignments for the protein nsp7. The 83 amino acid nsp7 protein is an essential cofactor in the RNA-dependent RNA polymerase. The polymerase activity and processivity of nsp12 are greatly enhanced by binding 1 copy of nsp7 and 2 copies of nsp8 to form a 160 kD complex. A separate hexadecameric complex of nsp7 and nsp8 (8 copies of each) forms a large ring-like structure. Thus, nsp7 is an important component of several large protein complexes that are required for replication of the large and complex coronavirus genome. We here report the near-complete NMR backbone and sidechain resonance assignment ((1)H,(13)C,(15)N) of isolated nsp7 from SARS-CoV-2 in solution. Further, we derive the secondary structure and compare it to the previously reported assignments and structure of the SARS-CoV nsp7. |*Magnetic Resonance Spectroscopy[MESH] |Carbon Isotopes[MESH] |Coronavirus RNA-Dependent RNA Polymerase/*chemistry[MESH] |Genome, Viral[MESH] |Hydrogen[MESH] |Hydrogen-Ion Concentration[MESH] |Nitrogen Isotopes[MESH] |Protein Binding[MESH] |Protein Domains[MESH] |Protein Structure, Secondary[MESH](1)H, (13)C, and (15)N backbone and side chain chemical shift assignme(epmc).pdf DeepDyve Pubget Overpricing