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10.1096/fj.202101670R http://scihub22266oqcxt.onion/10.1096/fj.202101670R 35157347!9111298!35157347     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=35157347&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 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\35157347.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       FASEB+J 2022 ; 36 (3): e22199 Nephropedia Template TP {{tp|p=35157347|t=2022. Structural polymorphism of coiled-coils from the stalk domain of SARS-CoV-2 spike protein |pdf=|usr=}}{{35157347}} gab.com Text Structural polymorphism of coiled-coils from the stalk domain of SARS-CoV-2 spike protein JO: FASEB J http://www.kidney.de/pget.php?&tw=1&pmid=35157347 #FOAvip Spike trimer plays a key role in SARS-CoV-2 infection and vaccine development. It consists of a globular head and a flexible stalk domain that anchors the protein into the viral membrane. While the head domain has been extensively studied, the properties of the adjoining stalk are poorly understood. Here, we characterize the coiled-coil formation and thermodynamic stability of the stalk domain and its segments. We find that the N-terminal segment of the stalk does not form coiled-coils and remains disordered in solution. The C-terminal stalk segment forms a trimeric coiled-coil in solution, which becomes significantly stabilized in the context of the full-length stalk. Its crystal structure reveals a novel antiparallel tetramer coiled-coil with an unusual combination of a-d and e-a-d hydrophobic core packing. Structural analysis shows that a subset of hydrophobic residues stabilizes different coiled-coil structures: trimer, tetramer, and heterohexamer, underscoring a highly polymorphic nature of the SARS-CoV-2 stalk sequence. Twit Text FOAVip Structural polymorphism of coiled-coils from the stalk domain of SARS-CoV-2 spike protein ????FASEB J http://www.kidney.de/pget.php?&tw=1&pmid=35157347 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=35157347 #FOAvip English Wikipedia <ref>{{Cite pmid|35157347}}</ref> Structural polymorphism of coiled-coils from the stalk domain of SARS-CoV-2 spike protein #MMPMID35157347 Zivic Z; Strmsek Z; Novinec M; Lah J; Hadzi S FASEB J 2022[Mar]; 36 (3): e22199 PMID35157347show ga Spike trimer plays a key role in SARS-CoV-2 infection and vaccine development. It consists of a globular head and a flexible stalk domain that anchors the protein into the viral membrane. While the head domain has been extensively studied, the properties of the adjoining stalk are poorly understood. Here, we characterize the coiled-coil formation and thermodynamic stability of the stalk domain and its segments. We find that the N-terminal segment of the stalk does not form coiled-coils and remains disordered in solution. The C-terminal stalk segment forms a trimeric coiled-coil in solution, which becomes significantly stabilized in the context of the full-length stalk. Its crystal structure reveals a novel antiparallel tetramer coiled-coil with an unusual combination of a-d and e-a-d hydrophobic core packing. Structural analysis shows that a subset of hydrophobic residues stabilizes different coiled-coil structures: trimer, tetramer, and heterohexamer, underscoring a highly polymorphic nature of the SARS-CoV-2 stalk sequence. |*Models, Molecular[MESH] |*Protein Domains[MESH] |Amino Acid Sequence[MESH] |COVID-19/*virology[MESH] |Crystallization[MESH] |Crystallography, X-Ray[MESH] |Humans[MESH] |Hydrophobic and Hydrophilic Interactions[MESH] |Protein Stability[MESH] |Protein Structure, Secondary[MESH] |SARS-CoV-2/*chemistry[MESH] |Scattering, Small Angle[MESH] |Spike Glycoprotein, Coronavirus/*chemistry[MESH] |Temperature[MESH]Structural polymorphism of coiled-coils from the stalk domain of SARS-(epmc).pdf DeepDyve Pubget Overpricing