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10.1007/s12104-020-09992-1 http://scihub22266oqcxt.onion/10.1007/s12104-020-09992-1 33392924!7779335!33392924     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 276.79999999999995 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 276.79999999999995 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biomol+NMR+Assign 2021 ; 15 (1): 107-116 Nephropedia Template TP {{tp|p=33392924|t=2021. Backbone chemical shift assignments for the SARS-CoV-2 non-structural protein Nsp9: intermediate (ms - mus) dynamics in the C-terminal helix at the dimer interface |pdf=|usr=}}{{33392924}} gab.com Text Backbone chemical shift assignments for the SARS-CoV-2 non-structural protein Nsp9: intermediate (ms - mus) dynamics in the C-terminal helix at the dimer interface JO: Biomol NMR Assign http://www.kidney.de/pget.php?&tw=1&pmid=33392924 #FOAvip The Betacoronavirus SARS-CoV-2 non-structural protein Nsp9 is a 113-residue protein that is essential for viral replication, and consequently, a potential target for the development of therapeutics against COVID19 infections. To capture insights into the dynamics of the protein's backbone in solution and accelerate the identification and mapping of ligand-binding surfaces through chemical shift perturbation studies, the backbone (1)H, (13)C, and (15)N NMR chemical shifts for Nsp9 have been extensively assigned. These assignments were assisted by the preparation of an ~ 70% deuterated sample and residue-specific, (15)N-labelled samples (V, L, M, F, and K). A major feature of the assignments was the "missing" amide resonances for N96-L106 in the (1)H-(15)N HSQC spectrum, a region that comprises almost the complete C-terminal alpha-helix that forms a major part of the homodimer interface in the crystal structure of SARS-CoV-2 Nsp9, suggesting this region either undergoes intermediate motion in the ms to mus timescale and/or is heterogenous. These "missing" amide resonances do not unambiguously appear in the (1)H-(15)N HSQC spectrum of SARS-CoV-2 Nsp9 collected at a concentration of 0.0007 mM. At this concentration, at the detection limit, native mass spectrometry indicates the protein is exclusively in the monomeric state, suggesting the intermediate motion in the C-terminal of Nsp9 may be due to intramolecular dynamics. Perhaps this intermediate ms to mus timescale dynamics is the physical basis for a previously suggested "fluidity" of the C-terminal helix that may be responsible for homophilic (Nsp9-Nsp9) and postulated heterophilic (Nsp9-Unknown) protein-protein interactions. Twit Text FOAVip Backbone chemical shift assignments for the SARS-CoV-2 non-structural protein Nsp9: intermediate (ms - mus) dynamics in the C-terminal helix at the dimer interface ????Biomol NMR Assign http://www.kidney.de/pget.php?&tw=1&pmid=33392924 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33392924 #FOAvip English Wikipedia <ref>{{Cite pmid|33392924}}</ref> Backbone chemical shift assignments for the SARS-CoV-2 non-structural protein Nsp9: intermediate (ms - mus) dynamics in the C-terminal helix at the dimer interface #MMPMID33392924 Buchko GW; Zhou M; Craig JK; Van Voorhis WC; Myler PJ Biomol NMR Assign 2021[Apr]; 15 (1): 107-116 PMID33392924show ga The Betacoronavirus SARS-CoV-2 non-structural protein Nsp9 is a 113-residue protein that is essential for viral replication, and consequently, a potential target for the development of therapeutics against COVID19 infections. To capture insights into the dynamics of the protein's backbone in solution and accelerate the identification and mapping of ligand-binding surfaces through chemical shift perturbation studies, the backbone (1)H, (13)C, and (15)N NMR chemical shifts for Nsp9 have been extensively assigned. These assignments were assisted by the preparation of an ~ 70% deuterated sample and residue-specific, (15)N-labelled samples (V, L, M, F, and K). A major feature of the assignments was the "missing" amide resonances for N96-L106 in the (1)H-(15)N HSQC spectrum, a region that comprises almost the complete C-terminal alpha-helix that forms a major part of the homodimer interface in the crystal structure of SARS-CoV-2 Nsp9, suggesting this region either undergoes intermediate motion in the ms to mus timescale and/or is heterogenous. These "missing" amide resonances do not unambiguously appear in the (1)H-(15)N HSQC spectrum of SARS-CoV-2 Nsp9 collected at a concentration of 0.0007 mM. At this concentration, at the detection limit, native mass spectrometry indicates the protein is exclusively in the monomeric state, suggesting the intermediate motion in the C-terminal of Nsp9 may be due to intramolecular dynamics. Perhaps this intermediate ms to mus timescale dynamics is the physical basis for a previously suggested "fluidity" of the C-terminal helix that may be responsible for homophilic (Nsp9-Nsp9) and postulated heterophilic (Nsp9-Unknown) protein-protein interactions. |*Magnetic Resonance Spectroscopy[MESH] |Binding Sites[MESH] |Carbon Isotopes[MESH] |Codon[MESH] |Crystallography, X-Ray[MESH] |Dimerization[MESH] |Disulfides[MESH] |Hydrogen[MESH] |Hydrogen-Ion Concentration[MESH] |Kinetics[MESH] |Ligands[MESH] |Nitrogen Isotopes[MESH] |Protein Binding[MESH] |Protein Domains[MESH] |Protein Structure, Secondary[MESH] |RNA-Binding Proteins/*chemistry[MESH] |SARS-CoV-2/*chemistry[MESH]Backbone chemical shift assignments for the SARS-CoV-2 non-structural (epmc).pdf DeepDyve Pubget Overpricing