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10.1093/bib/bbab056 http://scihub22266oqcxt.onion/10.1093/bib/bbab056 33634309!8108619!33634309     free     free     free 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       Brief+Bioinform 2021 ; 22 (2): 1499-1507 Nephropedia Template TP {{tp|p=33634309|t=2021. A model for pH coupling of the SARS-CoV-2 spike protein open/closed equilibrium |pdf=|usr=}}{{33634309}} gab.com Text A model for pH coupling of the SARS-CoV-2 spike protein open/closed equilibrium JO: Brief Bioinform http://www.kidney.de/pget.php?&tw=1&pmid=33634309 #FOAvip Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), causative agent of the coronavirus disease 2019 (COVID-19) pandemic, is thought to release its RNA genome at either the cell surface or within endosomes, the balance being dependent on spike protein stability, and the complement of receptors, co-receptors and proteases. To investigate possible mediators of pH-dependence, pKa calculations have been made on a set of structures for spike protein ectodomain and fragments from SARS-CoV-2 and other coronaviruses. Dominating a heat map of the aggregated predictions, three histidine residues in S2 are consistently predicted as destabilizing in pre-fusion (all three) and post-fusion (two of the three) structures. Other predicted features include the more moderate energetics of surface salt-bridge interactions and sidechain-mainchain interactions. Two aspartic acid residues in partially buried salt-bridges (D290-R273 and R355-D398) have pKas that are calculated to be elevated and destabilizing in more open forms of the spike trimer. These aspartic acids are most stabilized in a tightly closed conformation that has been observed when linoleic acid is bound, and which also affects the interactions of D614. The D614G mutation is known to modulate the balance of closed to open trimer. It is suggested that D398 in particular contributes to a pH-dependence of the open/closed equilibrium, potentially coupled to the effects of linoleic acid binding and D614G mutation, and possibly also A570D mutation. These observations are discussed in the context of SARS-CoV-2 infection, mutagenesis studies, and other human coronaviruses. Twit Text FOAVip A model for pH coupling of the SARS-CoV-2 spike protein open/closed equilibrium ????Brief Bioinform http://www.kidney.de/pget.php?&tw=1&pmid=33634309 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33634309 #FOAvip English Wikipedia <ref>{{Cite pmid|33634309}}</ref> A model for pH coupling of the SARS-CoV-2 spike protein open/closed equilibrium #MMPMID33634309 Warwicker J Brief Bioinform 2021[Mar]; 22 (2): 1499-1507 PMID33634309show ga Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), causative agent of the coronavirus disease 2019 (COVID-19) pandemic, is thought to release its RNA genome at either the cell surface or within endosomes, the balance being dependent on spike protein stability, and the complement of receptors, co-receptors and proteases. To investigate possible mediators of pH-dependence, pKa calculations have been made on a set of structures for spike protein ectodomain and fragments from SARS-CoV-2 and other coronaviruses. Dominating a heat map of the aggregated predictions, three histidine residues in S2 are consistently predicted as destabilizing in pre-fusion (all three) and post-fusion (two of the three) structures. Other predicted features include the more moderate energetics of surface salt-bridge interactions and sidechain-mainchain interactions. Two aspartic acid residues in partially buried salt-bridges (D290-R273 and R355-D398) have pKas that are calculated to be elevated and destabilizing in more open forms of the spike trimer. These aspartic acids are most stabilized in a tightly closed conformation that has been observed when linoleic acid is bound, and which also affects the interactions of D614. The D614G mutation is known to modulate the balance of closed to open trimer. It is suggested that D398 in particular contributes to a pH-dependence of the open/closed equilibrium, potentially coupled to the effects of linoleic acid binding and D614G mutation, and possibly also A570D mutation. These observations are discussed in the context of SARS-CoV-2 infection, mutagenesis studies, and other human coronaviruses. |*Hydrogen-Ion Concentration[MESH] |Amino Acid Sequence[MESH] |Humans[MESH] |Protein Conformation[MESH] |SARS-CoV-2/*metabolism[MESH] |Sequence Homology, Amino Acid[MESH] |Spike Glycoprotein, Coronavirus/chemistry/*metabolism[MESH]A model for pH coupling of the SARS-CoV-2 spike protein open/closed eq(epmc).pdf DeepDyve Pubget Overpricing