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10.1002/pro.736 http://scihub22266oqcxt.onion/10.1002/pro.736 21922588!3302656!21922588     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\21922588.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Protein+Sci 2011 ; 20 (12): 2125-9 Nephropedia Template TP {{tp|p=21922588|t=2011. SARS-CoV heptad repeat 2 is a trimer of parallel helices |pdf=|usr=}}{{21922588}} gab.com Text SARS-CoV heptad repeat 2 is a trimer of parallel helices JO: Protein Sci http://www.kidney.de/pget.php?&tw=1&pmid=21922588 #FOAvip In severe acute respiratory syndrome coronavirus, the envelope heptad repeat 2 (HR2) plays a critical role in viral entry. Moreover, HR2 is both the target for novel antiviral therapies and, as an isolated peptide, presents a potential antiviral therapeutic. The structure of HR2, as determined by NMR spectroscopy in the presence of the co-solvent trifluoroethanol (TFE), is a trimer of parallel helices, whereas the structure of HR2, as determined by X-ray crystallography, is a tetramer of anti-parallel helices. In this work, we added a nitroxide spin label to the N-terminal region of HR2 and used paramagnetic relaxation enhancement to assess the orientation of the HR2 helices under different solution conditions. We find that the relaxation effects are consistent with an orientation corresponding to a trimer of parallel helices in both the presence and absence of TFE. This work suggests that the different orientation and oligomerization states observed by NMR and X-ray are due to the 11 additional residues present at the N-terminus of the NMR construct. Twit Text FOAVip SARS-CoV heptad repeat 2 is a trimer of parallel helices ????Protein Sci http://www.kidney.de/pget.php?&tw=1&pmid=21922588 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=21922588 #FOAvip English Wikipedia <ref>{{Cite pmid|21922588}}</ref> SARS-CoV heptad repeat 2 is a trimer of parallel helices #MMPMID21922588 Celigoy J; Ramirez B; Caffrey M Protein Sci 2011[Dec]; 20 (12): 2125-9 PMID21922588show ga In severe acute respiratory syndrome coronavirus, the envelope heptad repeat 2 (HR2) plays a critical role in viral entry. Moreover, HR2 is both the target for novel antiviral therapies and, as an isolated peptide, presents a potential antiviral therapeutic. The structure of HR2, as determined by NMR spectroscopy in the presence of the co-solvent trifluoroethanol (TFE), is a trimer of parallel helices, whereas the structure of HR2, as determined by X-ray crystallography, is a tetramer of anti-parallel helices. In this work, we added a nitroxide spin label to the N-terminal region of HR2 and used paramagnetic relaxation enhancement to assess the orientation of the HR2 helices under different solution conditions. We find that the relaxation effects are consistent with an orientation corresponding to a trimer of parallel helices in both the presence and absence of TFE. This work suggests that the different orientation and oligomerization states observed by NMR and X-ray are due to the 11 additional residues present at the N-terminus of the NMR construct. |*Nuclear Magnetic Resonance, Biomolecular[MESH] |Models, Molecular[MESH] |Protein Multimerization[MESH] |Protein Structure, Secondary[MESH] |Severe Acute Respiratory Syndrome/virology[MESH] |Severe acute respiratory syndrome-related coronavirus/*chemistry[MESH] |Spin Labels[MESH]SARS-CoV heptad repeat 2 is a trimer of parallel helices (epmc).pdf DeepDyve Pubget Overpricing